polyclonal anti actin  (Millipore)


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    Name:
    Anti ACTB antibody
    Description:
    Actin a highly conserved protein is a major component of both the cytoskeletal and contractile structures in all cell types It varies in amount being related to the type of differentiation and to the functional state of cells and tissues Actin can be found in two different forms of aggregation the globular or the fibrillar state and at least six distinct isoforms occur in vertebrates The actins exhibit over 90 sequence homology but each isoform has a unique NH2 terminal sequence The isoforms are comprised of three alpha actins skeletal cardiac smooth one beta actin beta non muscle and two gamma actins gamma smooth muscle and gamma non muscle Difficulties have been encountered in producing polyclonal antibodies due to the highly conserved nature of actin
    Catalog Number:
    av40173
    Price:
    None
    Applications:
    beta-actin is a nonmuscle actin involved in cytoskeletal structures. Anti-ACTB (anti-beta-Actin) is a rabbit IgG polyclonal antibody used to tag beta-Actin protein(s) for detection and quantitation by Western blotting and in cells and tissues by immunohistochemical (IHC) techniques. Rabbit Anti-ActinB is useful for studying actin structure and function, and to probe binding sites of actin-binding proteins.
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    Structured Review

    Millipore polyclonal anti actin
    Anti ACTB antibody
    Actin a highly conserved protein is a major component of both the cytoskeletal and contractile structures in all cell types It varies in amount being related to the type of differentiation and to the functional state of cells and tissues Actin can be found in two different forms of aggregation the globular or the fibrillar state and at least six distinct isoforms occur in vertebrates The actins exhibit over 90 sequence homology but each isoform has a unique NH2 terminal sequence The isoforms are comprised of three alpha actins skeletal cardiac smooth one beta actin beta non muscle and two gamma actins gamma smooth muscle and gamma non muscle Difficulties have been encountered in producing polyclonal antibodies due to the highly conserved nature of actin
    https://www.bioz.com/result/polyclonal anti actin/product/Millipore
    Average 99 stars, based on 43 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti actin - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Mutation of I696 and W697 in the TRP box of vanilloid receptor subtype I modulates allosteric channel activation"

    Article Title: Mutation of I696 and W697 in the TRP box of vanilloid receptor subtype I modulates allosteric channel activation

    Journal: The Journal of General Physiology

    doi: 10.1085/jgp.201311070

    Mutation of I696X and W697X does not abrogate receptor surface expression. (A and B) Total and surface expression of representative I696X (A) and W697X (B) mutants. TRPV1 species were transiently expressed in HEK293 cells. At 48 h, cells were harvested, membrane proteins were biotinylated and purified by agarose-Streptavidin, and protein expression was analyzed by Western immunoblotting using a polyclonal anti-TRPV1 antibody. Whole cell and avidin-purified extracts were separated in 10% SDS-PAGE gels, electrotransferred to a PVDF membrane, and probed with the anti-TRPV1 antibody. Immunoblots were visualized with the ECL system. C and D denote the quantification expressed as the surface/total protein ratio of bands shown in A and B. Actin was used as a loading control. Mutants were chosen to represent the amino acid families. Data represent mean ± SEM (error bars), with n (number of independent experiments) = 3. *, P
    Figure Legend Snippet: Mutation of I696X and W697X does not abrogate receptor surface expression. (A and B) Total and surface expression of representative I696X (A) and W697X (B) mutants. TRPV1 species were transiently expressed in HEK293 cells. At 48 h, cells were harvested, membrane proteins were biotinylated and purified by agarose-Streptavidin, and protein expression was analyzed by Western immunoblotting using a polyclonal anti-TRPV1 antibody. Whole cell and avidin-purified extracts were separated in 10% SDS-PAGE gels, electrotransferred to a PVDF membrane, and probed with the anti-TRPV1 antibody. Immunoblots were visualized with the ECL system. C and D denote the quantification expressed as the surface/total protein ratio of bands shown in A and B. Actin was used as a loading control. Mutants were chosen to represent the amino acid families. Data represent mean ± SEM (error bars), with n (number of independent experiments) = 3. *, P

    Techniques Used: Mutagenesis, Expressing, Purification, Western Blot, Avidin-Biotin Assay, SDS Page

    2) Product Images from "The death substrate Gas2 binds m-calpain and increases susceptibility to p53-dependent apoptosis"

    Article Title: The death substrate Gas2 binds m-calpain and increases susceptibility to p53-dependent apoptosis

    Journal: The EMBO Journal

    doi: 10.1093/emboj/20.11.2702

    Fig. 7. Gas2Δ171–314 decreases endogenous p53 levels and its transcriptional activity. ( A ) U2OS cells were transfected with GFP, Mdm2 or Gas2Δ171–314 as indicated. Western blotting of total lysates was performed with DO-1 to monitor the p53 levels, with anti-Gas2 antibody to confirm the expression of transfected Gas2 and polyclonal anti-actin antibody as loading control. ( B ) U2OS cells were transfected with the p21-Luc reporter together with a control vector, GasΔ171–314 or Mdm2. Luciferase assays were performed 24 h later. Data represent arithmetic means ± SD from three independent experiments. ( C ) p53 –/– or p53 –/– Mdm2 –/– MEFs were transfected with the p21-Luc reporter together with GFP or GFP-tagged Gas2Δ171–314. Luciferase assays were performed 24 h later. Data represent arithmetic means ± SD from five independent experiments. ( D ) Diagram showing the viability of Balb/C 3T3 cells microinjected with GFP or GFP-tagged Gas2Δ171–314 after UV damage and in conditions where Gas2wt is physiologic ally induced. After microinjection and Gas2 induction, cells were treated with UV and 12 h later GFP staining was visualized to calculate cell recovery. ( E ) Diagram showing the apoptotic susceptibility of wild-type or p53 –/– MEFs transfected with GFP or GFP-tagged Gas2Δ171–314 after UV damage and in conditions where Gas2wt is physiologically induced. After transfection and Gas2 induction, cells were treated with UV and 12 h later GFP staining was visualized to calculate cell recovery.
    Figure Legend Snippet: Fig. 7. Gas2Δ171–314 decreases endogenous p53 levels and its transcriptional activity. ( A ) U2OS cells were transfected with GFP, Mdm2 or Gas2Δ171–314 as indicated. Western blotting of total lysates was performed with DO-1 to monitor the p53 levels, with anti-Gas2 antibody to confirm the expression of transfected Gas2 and polyclonal anti-actin antibody as loading control. ( B ) U2OS cells were transfected with the p21-Luc reporter together with a control vector, GasΔ171–314 or Mdm2. Luciferase assays were performed 24 h later. Data represent arithmetic means ± SD from three independent experiments. ( C ) p53 –/– or p53 –/– Mdm2 –/– MEFs were transfected with the p21-Luc reporter together with GFP or GFP-tagged Gas2Δ171–314. Luciferase assays were performed 24 h later. Data represent arithmetic means ± SD from five independent experiments. ( D ) Diagram showing the viability of Balb/C 3T3 cells microinjected with GFP or GFP-tagged Gas2Δ171–314 after UV damage and in conditions where Gas2wt is physiologic ally induced. After microinjection and Gas2 induction, cells were treated with UV and 12 h later GFP staining was visualized to calculate cell recovery. ( E ) Diagram showing the apoptotic susceptibility of wild-type or p53 –/– MEFs transfected with GFP or GFP-tagged Gas2Δ171–314 after UV damage and in conditions where Gas2wt is physiologically induced. After transfection and Gas2 induction, cells were treated with UV and 12 h later GFP staining was visualized to calculate cell recovery.

    Techniques Used: Activity Assay, Transfection, Western Blot, Expressing, Plasmid Preparation, Luciferase, Staining

    3) Product Images from "Lamina-associated polypeptide 2? regulates cell cycle progression and differentiation via the retinoblastoma-E2F pathway"

    Article Title: Lamina-associated polypeptide 2? regulates cell cycle progression and differentiation via the retinoblastoma-E2F pathway

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200511149

    LAP2α binds to Rb at its COOH terminus and associates with Rb, lamin A/C, and E2F promoter sequences in vivo. (A) Schematic drawing of LAP2α and LAP2α fragments used for binding studies and localization of molecular domains and interaction regions with Rb and lamins A/C in the polypeptide. Numbers denote amino acid positions; +, interaction; −, no interaction of respective LAP2α fragments with Rb. Light gray boxes denote the constant LAP2 regions, including LEM-like and LEM domains (hatched). Medium gray denotes the α-specific region, whereas dark gray indicates the chromatin interaction domain. On the right, in vitro–translated 35 S-labeled Rb was overlaid onto transblotted recombinant LAP2α fragments. A Ponceau S stain of the respective blot and an autoradiogram of the overlay are shown. Numbers on the right indicate molecular masses in kD. (B) HeLa cells stably expressing LAP2α-GFP were fixed in formaldehyde, mechanically lysed by sonication, and LAP2α was immunoprecipitated using monoclonal (m) or polyclonal (p) antibody to LAP2α. Control precipitations were performed with antibody-free medium (ctrl) and with preimmune serum (PI). Immunoblots of immunoprecipitates and respective inputs (IP, diluted 1:10) with antiserum to LAP2α, Rb, or monoclonal antibody to lamin A/C are shown. (C) Chromatin immunoprecipitation was performed from HeLa and 3T3 cells using monoclonal and polyclonal antibody to LAP2α, preimmune serum, or anti-acetylhistone H4 (H4), and E2F-dependent promoter sequences in the cyclin D1 and thymidine kinase (TK) genes were amplified by PCR. As a negative control, the presence of histone H4 or E-cadherin promoter sequences was tested. Ethidium bromide–stained DNA fragments in agarose gels are shown. IP, 1% input.
    Figure Legend Snippet: LAP2α binds to Rb at its COOH terminus and associates with Rb, lamin A/C, and E2F promoter sequences in vivo. (A) Schematic drawing of LAP2α and LAP2α fragments used for binding studies and localization of molecular domains and interaction regions with Rb and lamins A/C in the polypeptide. Numbers denote amino acid positions; +, interaction; −, no interaction of respective LAP2α fragments with Rb. Light gray boxes denote the constant LAP2 regions, including LEM-like and LEM domains (hatched). Medium gray denotes the α-specific region, whereas dark gray indicates the chromatin interaction domain. On the right, in vitro–translated 35 S-labeled Rb was overlaid onto transblotted recombinant LAP2α fragments. A Ponceau S stain of the respective blot and an autoradiogram of the overlay are shown. Numbers on the right indicate molecular masses in kD. (B) HeLa cells stably expressing LAP2α-GFP were fixed in formaldehyde, mechanically lysed by sonication, and LAP2α was immunoprecipitated using monoclonal (m) or polyclonal (p) antibody to LAP2α. Control precipitations were performed with antibody-free medium (ctrl) and with preimmune serum (PI). Immunoblots of immunoprecipitates and respective inputs (IP, diluted 1:10) with antiserum to LAP2α, Rb, or monoclonal antibody to lamin A/C are shown. (C) Chromatin immunoprecipitation was performed from HeLa and 3T3 cells using monoclonal and polyclonal antibody to LAP2α, preimmune serum, or anti-acetylhistone H4 (H4), and E2F-dependent promoter sequences in the cyclin D1 and thymidine kinase (TK) genes were amplified by PCR. As a negative control, the presence of histone H4 or E-cadherin promoter sequences was tested. Ethidium bromide–stained DNA fragments in agarose gels are shown. IP, 1% input.

    Techniques Used: In Vivo, Binding Assay, In Vitro, Labeling, Recombinant, Staining, Stable Transfection, Expressing, Sonication, Immunoprecipitation, Western Blot, Chromatin Immunoprecipitation, Amplification, Polymerase Chain Reaction, Negative Control

    4) Product Images from "Monoclonal antibody to novel cell surface epitope on Hsc70 promotes morphogenesis of bile ducts in newborn rat liver"

    Article Title: Monoclonal antibody to novel cell surface epitope on Hsc70 promotes morphogenesis of bile ducts in newborn rat liver

    Journal: Cell Stress & Chaperones

    doi: 10.1007/s12192-009-0120-2

    Immunoblotted MAb OC.10 reacts with Hsc70 protein. Recombinant bovine Hsc70 ( lanes 1–3 ) and recombinant Hsp70 ( lanes 5–7 ) proteins were immunoblotted with MAb OC.10 ( a ), monoclonal anti-Hsc70 ( b ), and polyclonal anti-Hsp70 ( c ). For each
    Figure Legend Snippet: Immunoblotted MAb OC.10 reacts with Hsc70 protein. Recombinant bovine Hsc70 ( lanes 1–3 ) and recombinant Hsp70 ( lanes 5–7 ) proteins were immunoblotted with MAb OC.10 ( a ), monoclonal anti-Hsc70 ( b ), and polyclonal anti-Hsp70 ( c ). For each

    Techniques Used: Recombinant

    5) Product Images from "Inhibitory Role of Plk1 in the Regulation of p73-dependent Apoptosis through Physical Interaction and Phosphorylation *Inhibitory Role of Plk1 in the Regulation of p73-dependent Apoptosis through Physical Interaction and Phosphorylation * S⃞"

    Article Title: Inhibitory Role of Plk1 in the Regulation of p73-dependent Apoptosis through Physical Interaction and Phosphorylation *Inhibitory Role of Plk1 in the Regulation of p73-dependent Apoptosis through Physical Interaction and Phosphorylation * S⃞

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M710608200

    Plk1 has an ability to phosphorylate p73 at its NH 2 -terminal region in vitro . A , Coomassie Brilliant Blue staining of GST or GST-p73α fusion proteins used for in vitro kinase reaction. B, in vitro kinase assay. GST or the indicated GST-p73α deletion mutants bound to glutathione-Sepharose beads were washed with washing buffer and resuspended in 90 μl of kinase reaction buffer. Protein X, which was supplied by manufacturer, was used as a positive control. 10 μl of the active form of Plk1 were added to the reaction mixtures and incubated at 30 °C for 30 min. The reaction mixtures were washed with washing buffer and then incubated with 100 μl of polyclonal anti-phospho-Thr antibody at room temperature for 30 min followed by incubation with horseradish peroxidase-conjugated anti-rabbit IgG at room temperature for 30 min. After incubation, 100 μl of substrate reagent were added to the reaction mixtures and incubated at room temperature for 5 min. Yellow coloration indicates the Plk1-mediated phosphorylation at Thr residue. After the addition of 100 μl of stop solution, supernatant was transferred into 96-well tissue culture plate, and the absorbance reading was carried out at 450/540 nm using the microplate reader ( C ).
    Figure Legend Snippet: Plk1 has an ability to phosphorylate p73 at its NH 2 -terminal region in vitro . A , Coomassie Brilliant Blue staining of GST or GST-p73α fusion proteins used for in vitro kinase reaction. B, in vitro kinase assay. GST or the indicated GST-p73α deletion mutants bound to glutathione-Sepharose beads were washed with washing buffer and resuspended in 90 μl of kinase reaction buffer. Protein X, which was supplied by manufacturer, was used as a positive control. 10 μl of the active form of Plk1 were added to the reaction mixtures and incubated at 30 °C for 30 min. The reaction mixtures were washed with washing buffer and then incubated with 100 μl of polyclonal anti-phospho-Thr antibody at room temperature for 30 min followed by incubation with horseradish peroxidase-conjugated anti-rabbit IgG at room temperature for 30 min. After incubation, 100 μl of substrate reagent were added to the reaction mixtures and incubated at room temperature for 5 min. Yellow coloration indicates the Plk1-mediated phosphorylation at Thr residue. After the addition of 100 μl of stop solution, supernatant was transferred into 96-well tissue culture plate, and the absorbance reading was carried out at 450/540 nm using the microplate reader ( C ).

    Techniques Used: In Vitro, Staining, Kinase Assay, Positive Control, Incubation

    6) Product Images from "Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer"

    Article Title: Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200312034

    Electron microscopic localization of mVPS26 and Snx1. HeLaM cells grown in 6-cm dishes were permeabilized by rapid freeze/thaw. After fixation, mVPS26 or Snx1 was labeled with polyclonal antisera followed by 10-nm colloidal gold anti–rabbit. The cells were embedded in Epon and then sectioned to produce ∼50-nm-thick sections. mVPS26 (a–c) and Snx1 (d and e) are found on multivesicular bodies characteristic of endosomal compartments. Bar, 250 nm. Arrows indicate Snx1 localization to tubular–vesicular structures.
    Figure Legend Snippet: Electron microscopic localization of mVPS26 and Snx1. HeLaM cells grown in 6-cm dishes were permeabilized by rapid freeze/thaw. After fixation, mVPS26 or Snx1 was labeled with polyclonal antisera followed by 10-nm colloidal gold anti–rabbit. The cells were embedded in Epon and then sectioned to produce ∼50-nm-thick sections. mVPS26 (a–c) and Snx1 (d and e) are found on multivesicular bodies characteristic of endosomal compartments. Bar, 250 nm. Arrows indicate Snx1 localization to tubular–vesicular structures.

    Techniques Used: Labeling

    Immunofluorescence localization of mVPS26. (A) HeLaM cells stably transfected with the respective CD8 reporter were fixed and labeled with polyclonal anti-mVPS26 and monoclonal anti-CD8 followed by secondary antibodies. Bar, 20 μm. (B) HeLaM cells stably expressing GFP-rab proteins were fixed and labeled with antisera against mVPS26 followed by fluorescently labeled secondary antibodies. Bar, 20 μm. Arrows indicate coincident labeling.
    Figure Legend Snippet: Immunofluorescence localization of mVPS26. (A) HeLaM cells stably transfected with the respective CD8 reporter were fixed and labeled with polyclonal anti-mVPS26 and monoclonal anti-CD8 followed by secondary antibodies. Bar, 20 μm. (B) HeLaM cells stably expressing GFP-rab proteins were fixed and labeled with antisera against mVPS26 followed by fluorescently labeled secondary antibodies. Bar, 20 μm. Arrows indicate coincident labeling.

    Techniques Used: Immunofluorescence, Stable Transfection, Transfection, Labeling, Expressing

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    Article Snippet: .. Rabbit anti-Cx43 polyclonal antibody (C6219), rabbit anti-caspase-3 polyclonal antibody (C9598), rabbit anti-survivin polyclonal antibody (SAB3500269), rabbit anti-α-tubulin polyclonal antibody (SAB4500087), rabbit anti-cyclin B1 polyclonal antibody (C8831), rabbit anti-β-actin polyclonal antibody (SAB2100037), anti-rabbit IgG-peroxidase antibody (SAB3700870), MTT, neomycin (G418) and paclitaxel were purchased from Sigma-Aldrich (Merck KGaA, Darmstadt, Germany). .. Rabbit anti-ATPase β3 (Na+ /K+ ) polyclonal antibody (GTX114272) was purchased from GeneTex, Inc. (Irvine, CA, USA).

    Isolation:

    Article Title: SETD7 Regulates the Differentiation of Human Embryonic Stem Cells
    Article Snippet: .. Western blot analysis Whole cell extracts were isolated using RIPA buffer and 30 μg protein was analyzed by western blot using specific antibodies against OCT4 (Santa Cruz sc-5279), SOX2 (Neuromics GT15098), α-1-Fetoprotein (AFP; Dako, A0008), SETD7 (Millipore 07–314), TUBA (Santa Cruz sc-135592), ACTB (Sigma AV40173) or FLAG (Sigma M2). .. Cell Cycle Analyses Cell cycle analyses were performed using Click-iT® EdU Alexa Fluor® 488 Flow Cytometry Assay Kit (Invitrogen) according to manufacturer instructions.

    Incubation:

    Article Title: Neuronal Nitric Oxide Synthase Contributes to PTZ Kindling Epilepsy-Induced Hippocampal Endoplasmic Reticulum Stress and Oxidative Damage
    Article Snippet: .. Next the membranes were incubated with mouse anti-3-NT (1:2,500; Abcam, Temecula, CA, USA, Cat# ab61392), rabbit anti-CHOP (1:2,000; Abcam, Temecula, CA, USA, Cat# ab179823), mouse anti-GRP78 (1:2,500; Santa Cruz, Texas, USA, Cat# sc373738) and rabbit anti-β-actin (1:5,000; Sigma-Aldrich, St, Louis, USA, Cat# SAB2100037) in TBST overnight at 4°C. .. The membranes were then washed with TBST and incubated with HRP-linked secondary antibody (Boster Bioengineering, Wuhan, China) diluted 1:5,000 for 1 h. Following several washes with TBST, the binding antibodies were detected with an enhanced chemiluminescence (ECL) reagents (Millipore, Billerica, MA, USA) by using a MicroChemi chemiluminescent image analysis system (DNR Bio-imaging Systems, Jerusalem, Israel).

    Expressing:

    Article Title: Influence of Cannabinoid Receptor Deficiency on Parameters Involved in Blood Glucose Regulation in Mice
    Article Snippet: .. The expression of beta-actin (Actb) was used to normalise the target genes. .. The identity of amplicons was verified by restriction analysis and agarose gel electrophoresis.

    Western Blot:

    Article Title: SETD7 Regulates the Differentiation of Human Embryonic Stem Cells
    Article Snippet: .. Western blot analysis Whole cell extracts were isolated using RIPA buffer and 30 μg protein was analyzed by western blot using specific antibodies against OCT4 (Santa Cruz sc-5279), SOX2 (Neuromics GT15098), α-1-Fetoprotein (AFP; Dako, A0008), SETD7 (Millipore 07–314), TUBA (Santa Cruz sc-135592), ACTB (Sigma AV40173) or FLAG (Sigma M2). .. Cell Cycle Analyses Cell cycle analyses were performed using Click-iT® EdU Alexa Fluor® 488 Flow Cytometry Assay Kit (Invitrogen) according to manufacturer instructions.

    Chloramphenicol Acetyltransferase Assay:

    Article Title: Loss of PARP-1 attenuates diabetic arteriosclerotic calcification via Stat1/Runx2 axis
    Article Snippet: .. The following primary antibodies were employed: anti-PARP-1 (1:500, Santa Cruz, CatSC-7150), anti-Runx2 (1:1000, Cell Signaling Technology, Cat#12556), anti-Bmp2 (1:1000, Abcam, Cat#ab14933), anti-Msx2 (1:1000, Sigma, Cat#HPA005652),anti-OPN (1:1000, Abcam, Cat#ab8448), anti-Stat1 (1:1000, Cell Signaling Technology, Cat#14994), anti-p-Stat1 (Tyr701, 1:1000, Cell Signaling Technology, Cat#5375), anti-vimentin (1:1000, Cell Signaling Technology, Cat# 5741), anti-α-SMA (1:1000, Abcam, Cat#ab32575), anti-iNOS (1:1000, Abcam, Cat#ab178945), anti-Arg1 (1:1000, Cell Signaling Technology, Cat#93668), and anti-β-actin (1:5000, Sigma, Cat#SAB2100037). .. Luciferase activity assay 293T cells were transiently cotransfected with a Runx2 promoter luciferase reporter plasmid (pGL3-Runx2-Luc) and a Renilla reporter plasmid (pRL-TK) using Lipofectamine 3000 transfection reagent (Invitrogen).

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  • 99
    Millipore anti fibronectin antibody
    Mechanism(s) leading to excessive generation of ROS following overexpression of MIOX under HG with ensuing increased apoptosis and synthesis of ECM <t>fibronectin.</t> MIOX overexpression (pcDNA transfection) in tubular cells generates excessive generation of
    Anti Fibronectin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 236 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti fibronectin antibody/product/Millipore
    Average 99 stars, based on 236 article reviews
    Price from $9.99 to $1999.99
    anti fibronectin antibody - by Bioz Stars, 2020-09
    99/100 stars
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    99
    Millipore anti β actin antiserum
    SNL resulted in upregulation of the NR1 and NR2B subunits of NMDARs, but not the GluR1 or GluR2 subunit of AMPARs in the vlPAG. Representative Western blots and summarized bar graphs depicting the expression level of GluR1 ( A ), GluR2 ( B ), NR1 ( C ), NR2A ( D ), or NR2B ( E ) subunit protein in vlPAG samples micropunched from sham, NP3, and NP10 rats. The top blots are the immunoreactive bands against the respective antibody against the GluR1, GluR2, NR1, NR2A, or NR2B subunit protein and the bottom blots are the bands for the housekeeping protein <t>β-actin.</t> The ordinate of the base graph is the expression level of the receptor protein, taking the sham group as 100%. * p
    Anti β Actin Antiserum, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti β actin antiserum/product/Millipore
    Average 99 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    anti β actin antiserum - by Bioz Stars, 2020-09
    99/100 stars
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    99
    Millipore rabbit polyclonal anti α sma
    mEVs modulate TGFβ1-induced myofibroblastic differentiation in a Thy-1-dependent manner. ( A ) Normal lung fibroblasts (NLF) or ( B ) IPF lung fibroblasts were made quiescent in serum free medium for 16 hrs and then incubated with TGF-β1 (2ng/ml, overnight), together with indicated EV preparations, and total RNA was subjected to RT-PCR using primers for human <t>α-SMA,</t> FN-EDA, collagen I, and collagen III. Gene expression is graphed as mean +/− SEM of ΔΔCt compared to unstimulated baseline for n = 4 biological replicates. *p
    Rabbit Polyclonal Anti α Sma, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti α sma/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti α sma - by Bioz Stars, 2020-09
    99/100 stars
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    Image Search Results


    Mechanism(s) leading to excessive generation of ROS following overexpression of MIOX under HG with ensuing increased apoptosis and synthesis of ECM fibronectin. MIOX overexpression (pcDNA transfection) in tubular cells generates excessive generation of

    Journal: The Journal of Biological Chemistry

    Article Title: myo-Inositol Oxygenase Overexpression Accentuates Generation of Reactive Oxygen Species and Exacerbates Cellular Injury following High Glucose Ambience

    doi: 10.1074/jbc.M115.669952

    Figure Lengend Snippet: Mechanism(s) leading to excessive generation of ROS following overexpression of MIOX under HG with ensuing increased apoptosis and synthesis of ECM fibronectin. MIOX overexpression (pcDNA transfection) in tubular cells generates excessive generation of

    Article Snippet: From Sigma-Aldrich, we purchased polyclonal anti-fibronectin (catalogue no. F3648), anti-cytochrome c (catalogue no. C9616), anti-superoxide dismutase 1 (SOD1) (catalogue no. HPA001401), anti-SOD2 (catalogue no. HPA001814), anti-heme oxygenase-1 (catalogue no. H4535), and monoclonal anti-β-actin (catalogue no. A5441) antibodies; NAD+ ; NADH; culture media; monobromobimane (MBB; reduced glutathione); diphenyleneiodonium chloride (DPI); N -acetylcysteine (NAC); and the caspase-3 assay kit.

    Techniques: Over Expression, Transfection

    SNL resulted in upregulation of the NR1 and NR2B subunits of NMDARs, but not the GluR1 or GluR2 subunit of AMPARs in the vlPAG. Representative Western blots and summarized bar graphs depicting the expression level of GluR1 ( A ), GluR2 ( B ), NR1 ( C ), NR2A ( D ), or NR2B ( E ) subunit protein in vlPAG samples micropunched from sham, NP3, and NP10 rats. The top blots are the immunoreactive bands against the respective antibody against the GluR1, GluR2, NR1, NR2A, or NR2B subunit protein and the bottom blots are the bands for the housekeeping protein β-actin. The ordinate of the base graph is the expression level of the receptor protein, taking the sham group as 100%. * p

    Journal: The Journal of Neuroscience

    Article Title: Hypofunction of Glutamatergic Neurotransmission in the Periaqueductal Gray Contributes to Nerve-Injury-Induced Neuropathic Pain

    doi: 10.1523/JNEUROSCI.5583-12.2013

    Figure Lengend Snippet: SNL resulted in upregulation of the NR1 and NR2B subunits of NMDARs, but not the GluR1 or GluR2 subunit of AMPARs in the vlPAG. Representative Western blots and summarized bar graphs depicting the expression level of GluR1 ( A ), GluR2 ( B ), NR1 ( C ), NR2A ( D ), or NR2B ( E ) subunit protein in vlPAG samples micropunched from sham, NP3, and NP10 rats. The top blots are the immunoreactive bands against the respective antibody against the GluR1, GluR2, NR1, NR2A, or NR2B subunit protein and the bottom blots are the bands for the housekeeping protein β-actin. The ordinate of the base graph is the expression level of the receptor protein, taking the sham group as 100%. * p

    Article Snippet: The loading and blotting of equal amounts of protein were verified by reprobing the membrane with anti-β-actin antiserum (1:1000, catalog #MAB1501, lot LV1435643; Millipore).

    Techniques: Western Blot, Expressing

    mEVs modulate TGFβ1-induced myofibroblastic differentiation in a Thy-1-dependent manner. ( A ) Normal lung fibroblasts (NLF) or ( B ) IPF lung fibroblasts were made quiescent in serum free medium for 16 hrs and then incubated with TGF-β1 (2ng/ml, overnight), together with indicated EV preparations, and total RNA was subjected to RT-PCR using primers for human α-SMA, FN-EDA, collagen I, and collagen III. Gene expression is graphed as mean +/− SEM of ΔΔCt compared to unstimulated baseline for n = 4 biological replicates. *p

    Journal: Scientific Reports

    Article Title: Thy-1 dependent uptake of mesenchymal stem cell-derived extracellular vesicles blocks myofibroblastic differentiation

    doi: 10.1038/s41598-017-18288-9

    Figure Lengend Snippet: mEVs modulate TGFβ1-induced myofibroblastic differentiation in a Thy-1-dependent manner. ( A ) Normal lung fibroblasts (NLF) or ( B ) IPF lung fibroblasts were made quiescent in serum free medium for 16 hrs and then incubated with TGF-β1 (2ng/ml, overnight), together with indicated EV preparations, and total RNA was subjected to RT-PCR using primers for human α-SMA, FN-EDA, collagen I, and collagen III. Gene expression is graphed as mean +/− SEM of ΔΔCt compared to unstimulated baseline for n = 4 biological replicates. *p

    Article Snippet: Monoclonal anti-FN-EDA (ab6328, Abcam, Cambridge, MA), monoclonal anti-collagen I (GTX26308, GeneTex) and rabbit polyclonal anti-α-SMA (CBL171-I, EMD Millipore, Temecula, CA) anti-collagen III (GTX111643, GeneTex) and anti-N-cadherin (GTX127345, GeneTex) were used in western blotting studies.

    Techniques: Incubation, Reverse Transcription Polymerase Chain Reaction, Expressing