rabbit polyclonal igg anti zip10  (ProSci Incorporated)


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    Structured Review

    ProSci Incorporated rabbit polyclonal igg anti zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Rabbit Polyclonal Igg Anti Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal igg anti zip10/product/ProSci Incorporated
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal igg anti zip10 - by Bioz Stars, 2023-09
    90/100 stars

    Images

    1) Product Images from "Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter"

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00573.2017

    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Figure Legend Snippet: Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Techniques Used: Sequencing, Amplification, Reverse Transcription Polymerase Chain Reaction, Functional Assay, Clone Assay, Microarray, Derivative Assay, Expressing

    63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.
    Figure Legend Snippet: 63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Techniques Used: Clone Assay, Expressing, Recombinant, Injection

    Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.
    Figure Legend Snippet: Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Techniques Used: Injection

    Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.
    Figure Legend Snippet: Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Techniques Used: Expressing, Injection, Immunohistochemistry, Recombinant

    ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.
    Figure Legend Snippet: ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Techniques Used: Expressing, Western Blot

    Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Techniques Used: Immunofluorescence, Staining

    Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Techniques Used: Immunohistochemistry, Labeling

    Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Techniques Used: Immunofluorescence, Labeling

    Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Techniques Used: Staining

    Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.
    Figure Legend Snippet: Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Techniques Used: Staining

    rabbit polyclonal igg anti zip10  (ProSci Incorporated)


    Bioz Verified Symbol ProSci Incorporated is a verified supplier
    Bioz Manufacturer Symbol ProSci Incorporated manufactures this product  
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    Structured Review

    ProSci Incorporated rabbit polyclonal igg anti zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Rabbit Polyclonal Igg Anti Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal igg anti zip10/product/ProSci Incorporated
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal igg anti zip10 - by Bioz Stars, 2023-09
    90/100 stars

    Images

    1) Product Images from "Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter"

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00573.2017

    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Figure Legend Snippet: Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Techniques Used: Sequencing, Amplification, Reverse Transcription Polymerase Chain Reaction, Functional Assay, Clone Assay, Microarray, Derivative Assay, Expressing

    63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.
    Figure Legend Snippet: 63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Techniques Used: Clone Assay, Expressing, Recombinant, Injection

    Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.
    Figure Legend Snippet: Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Techniques Used: Injection

    Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.
    Figure Legend Snippet: Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Techniques Used: Expressing, Injection, Immunohistochemistry, Recombinant

    ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.
    Figure Legend Snippet: ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Techniques Used: Expressing, Western Blot

    Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Techniques Used: Immunofluorescence, Staining

    Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Techniques Used: Immunohistochemistry, Labeling

    Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Techniques Used: Immunofluorescence, Labeling

    Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Techniques Used: Staining

    Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.
    Figure Legend Snippet: Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Techniques Used: Staining

    rabbit polyclonal igg anti zip10  (ProSci Incorporated)


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    ProSci Incorporated rabbit polyclonal igg anti zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Rabbit Polyclonal Igg Anti Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal igg anti zip10/product/ProSci Incorporated
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal igg anti zip10 - by Bioz Stars, 2023-09
    90/100 stars

    Images

    1) Product Images from "Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter"

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00573.2017

    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Figure Legend Snippet: Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Techniques Used: Sequencing, Amplification, Reverse Transcription Polymerase Chain Reaction, Functional Assay, Clone Assay, Microarray, Derivative Assay, Expressing

    63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.
    Figure Legend Snippet: 63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Techniques Used: Clone Assay, Expressing, Recombinant, Injection

    Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.
    Figure Legend Snippet: Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Techniques Used: Injection

    Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.
    Figure Legend Snippet: Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Techniques Used: Expressing, Injection, Immunohistochemistry, Recombinant

    ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.
    Figure Legend Snippet: ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Techniques Used: Expressing, Western Blot

    Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Techniques Used: Immunofluorescence, Staining

    Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Techniques Used: Immunohistochemistry, Labeling

    Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Techniques Used: Immunofluorescence, Labeling

    Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Techniques Used: Staining

    Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.
    Figure Legend Snippet: Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Techniques Used: Staining

    rabbit polyclonal igg anti zip10  (ProSci Incorporated)


    Bioz Verified Symbol ProSci Incorporated is a verified supplier
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    Structured Review

    ProSci Incorporated rabbit polyclonal igg anti zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Rabbit Polyclonal Igg Anti Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal igg anti zip10/product/ProSci Incorporated
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal igg anti zip10 - by Bioz Stars, 2023-09
    90/100 stars

    Images

    1) Product Images from "Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter"

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00573.2017

    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Figure Legend Snippet: Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Techniques Used: Sequencing, Amplification, Reverse Transcription Polymerase Chain Reaction, Functional Assay, Clone Assay, Microarray, Derivative Assay, Expressing

    63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.
    Figure Legend Snippet: 63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Techniques Used: Clone Assay, Expressing, Recombinant, Injection

    Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.
    Figure Legend Snippet: Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Techniques Used: Injection

    Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.
    Figure Legend Snippet: Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Techniques Used: Expressing, Injection, Immunohistochemistry, Recombinant

    ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.
    Figure Legend Snippet: ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Techniques Used: Expressing, Western Blot

    Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Techniques Used: Immunofluorescence, Staining

    Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Techniques Used: Immunohistochemistry, Labeling

    Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Techniques Used: Immunofluorescence, Labeling

    Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.
    Figure Legend Snippet: Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Techniques Used: Staining

    Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.
    Figure Legend Snippet: Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Techniques Used: Staining

    anti rabbit zip10  (ProSci Incorporated)


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    ProSci Incorporated anti rabbit zip10
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    ProSci Incorporated anti rabbit zip10
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    https://www.bioz.com/result/anti rabbit zip10/product/ProSci Incorporated
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    ProSci Incorporated rabbit polyclonal igg anti zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Rabbit Polyclonal Igg Anti Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ProSci Incorporated anti rabbit zip10
    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly <t>ZIP10).</t> Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).
    Anti Rabbit Zip10, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti rabbit zip10/product/ProSci Incorporated
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Slc39a10 sequence analyses. A: sequence pileup of human SLC39A10 (H; NM_001127257), dog slc39a10 (D; KY094513), mouse (M; NP_76624), and Drosophila (CG10006; dZip71B, fly ZIP10). Human, dog, mouse, and Drosophila ZIP10 cDNAs were amplified from kidney (human, dog, and mouse) or whole body (fly) by RT-PCR using gene-specific primers based on 5′ and 3′ expressed sequence tag primers. Black shading indicates identical amino acids in all four (human, dog, mouse, and fly) gene products, whereas gray shading indicates similar functional groups. B: identity and divergence analysis of ZIP10 clones. C: distribution of CG10006 mRNA in larval (left) and adult (right) Drosophila. Data are mined from FlyAtlas.org, an Affymetrix microarray-derived expression atlas of Drosophila (4).

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Sequencing, Amplification, Reverse Transcription Polymerase Chain Reaction, Functional Assay, Clone Assay, Microarray, Derivative Assay, Expressing

    63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: 63Zn2+ uptake by ZIP10 clones in Xenopus laevis oocytes expressing recombinant human, dog, or Drosophila ZIP10. A: Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) and water controls were used for 63Zn2+ uptake. The data from the pH 7.5 uptake solution is shown. All species had significant uptake (P < 0.001) compared with water, and no interspecies differences were detected (P > 0.05), as determined by ANOVA with Tukey’s post hoc test. B: the same four groups of oocytes were placed in six different solutions with varying isoosmotic ion replacements, and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates with a total n = 120 oocytes per species. Log-scaled data are shown. Xenopus laevis oocytes injected with cRNA coding for either human, dog, or fly (Drosophila) ZIP10 (Slc39a10) were placed in either pH 7.5 ND90/96 (black symbols), pH 8.5 ND90/96, pH 8.5 HCO3−, pH 7.5 0 mM Na+, pH 7.5 0 mM Cl−, or pH 7.5 KCl (high potassium), and 63Zn2+ uptake was measured in nanomoles per hour per oocyte; n = 10 oocytes per solution done in two replicates. Log-scaled data are shown. 63Zn2+ uptake did not differ significantly between solutions for any species (P > 0.05), as determined by ANOVA with Tukey’s post hoc test.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Clone Assay, Expressing, Recombinant, Injection

    Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Electrophysiology characterization of ZIP10 in Xenopus oocytes. Xenopus oocytes were injected with human ZIP10 cRNA. A: nonvoltage clamped experiment in which intracellular pH (pHi) and membrane potential (Vm) were measured, and 1 mM ZnCl2 (blue shading) was added in the absence or presence of 5% CO2:33 mM HCO3− (pH 7.5; tan shading). B and C: similar experiments in which pHi is measured while the oocytes is clamped at −20 mV. D: current-voltage curves of ZIP10 oocytes with 0 mM Zn2+ (ND96), 1 mM Zn2+, and 5 mM Zn2+. The red-dotted circle in C indicates an air bubble in the system, which also manifests as a quick current spike. The repeat maneuver shows no pHi or current change.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Injection

    Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Human, dog, and Drosophila ZIP10 expression in Xenopus oocyte plasma membrane. Xenopus laevis oocytes were injected with cRNA coding for either water (control; A), dog ZIP10 (B), human ZIP10 (C), or dZIP10 (CG10006; D). To determine whether a commercially available ZIP10 antibody would detect the expressed Zip proteins, oocytes were processed using immunohistochemistry 3–5 days after cRNA injection. Fluorescent immunohistochemistry shows recognition of recombinant protein epitopes across species (red: human, dog, and fly), but not water-injected control. DAPI denotes cell interior as counterstain (blue). Magnification is at ×20.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Expressing, Injection, Immunohistochemistry, Recombinant

    ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: ZIP10 (Slc39A10) expression in normal mouse (M), dog (D), and human (H) kidney. A: immunoblot analysis of ZIP10 expressions in kidneys from normal mouse, dog, and human tissue. The apparent molecular mass for mouse, dog, and human ZIP10 (94 kDa) is the same across species and matches the reported weight recognized by the rabbit polyclonal antibody. B: graphical representation of ZIP10 protein levels normalized to β-actin loading controls.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Expressing, Western Blot

    Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Immunofluorescent detection of mouse ZIP10 (Slc39a10). A: immunofluorescence of mouse kidney section costained with Zip10 (red) and monocarboxylate transporter-1 [MCT-1; green; basolateral membrane of proximal tubules (PT)]. Note there is additional apical Zip10 staining. B: immunofluorescence of a mouse kidney section costained with Zip10 (red) and aquaporin-2 [AQP-2; yellow; apical membrane of collecting duct (CD)]. DAPI denotes PT cell nuclei (blue). C: midcortical section of mouse kidney stained with Zip10 (red), LTA [lotus tetragonolobus agglutinin; green; glycocaylx of PT), and uromodulin (UMOD or Tamm Horsfall; white; thick ascending limb]. D: cortical section of mouse kidney stained with Zip10 (red) and LTA (green; glycocaylx of PT). Bars = 100 µm.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Immunofluorescence, Staining

    Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Immunofluorescent detection of ZIP10 in the Drosophila Malpighian tubule (MT). A: immunohistochemistry showing specific labeling of ZIP10 (red) in the MT lumen in a wild-type (WT) Oregon R female, anterior MT. B: when CG10006-RNAi is driven by CapaR-Gal4 (MT principal cells), there is no specific labeling with the ZIP10 antibody, which does recognize the Drosophila epitope (Fig. 3D). DAPI denotes principal and stellate cell nuclei (blue). Magnification is at ×20.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Immunohistochemistry, Labeling

    Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Immunofluorescent detection of ZIP10 (Slc39a10) in normal dog kidney. A: immunofluorescence showing specific labeling of dog ZIP10 (red) on the apical membrane of proximal tubule cells colocalized with monocarboxylate transporter-1 (MCT-1; green; basolateral membrane). B: cortical section of dog kidney costained with Zip10 (red), Na+-K+-2Cl− cotransporter 2 [NKCC2; green, apical, thick ascending limb (TAL)], and uromodulin (UMOD; white; TAL). C: near-medullary section of dog kidney costained with Zip10, NKCC2, and Tamm Horsfall showing clear TAL segments. D: immunofluorescence colocalizing ZIP10 with aquaporin-2 (AQP-2; yellow) marking the apical membrane of cortical collecting duct (CCD) cells. E and F: ZIP10 and AQP-2 alone, respectively, from D. DAPI denotes cell nuclei (blue). Bar = 100 µm.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Immunofluorescence, Labeling

    Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Immunofluorescent detection of ZIP10 (SLC39A10) in normal, adult human kidney. Immunofluorescent staining of normal human kidney sections is shown. The white bar in each panel is 100 µm. A: costaining of ZIP10 (red), monocarboxylate transporter-1 [MCT-1; green; proximal tubule (PT)], and DAPI. Obviously costained PTs are indicated. B: costaining using ZIP10 (red), MCT-1 (green; PT), and Na+-K+-2Cl− cotransporter 2 [NKCC2; white; thick ascending limb (TAL)]. C: costaining using ZIP10 (red), lotus tetragonolobus agglutinin (LTA; green; PT), and uromodulin (UMOD; white; TAL). D: as in Fig. 8 (dog kidney) shows colocalization of ZIP10 (red) and AQP-2 (yellow; CD) in some but not all tubules. DAPI denotes cell nuclei (blue). CCD, cortical collecting duct.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Staining

    Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Cloning, function, and localization of human, canine, and Drosophila ZIP10 (SLC39A10), a Zn 2+ transporter

    doi: 10.1152/ajprenal.00573.2017

    Figure Lengend Snippet: Nephron cartoon summarizing differences between mouse and dog/human Zip10 staining. Two nephron diagrams show Zip10 reactivity: mouse (left) and dog or human (right). The thick red line indicates tubule areas where ZIP10 protein staining was found. CCD, cortical collecting duct; DT, distal tubule; IMCD, inner medullary collecting duct; TAL, thick ascending limb.

    Article Snippet: Sections were incubated with rabbit polyclonal IgG anti-ZIP10 (no. 6099; primary; ProSci, Poway, CA) at 4°C overnight and allowed to incubate at room temperature (RT) with goat-anti-rabbit-AF568 (secondary).

    Techniques: Staining