rabbit polyclonal anti syt 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti syt 1
    <t>SYT-1</t> protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.
    Rabbit Polyclonal Anti Syt 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti syt 1/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti syt 1 - by Bioz Stars, 2023-02
    92/100 stars

    Images

    1) Product Images from "An altered glial phenotype in the NL3 R451C mouse model of autism"

    Article Title: An altered glial phenotype in the NL3 R451C mouse model of autism

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-71171-y

    SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.
    Figure Legend Snippet: SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.

    Techniques Used: Expressing, Western Blot, Two Tailed Test

    Antibodies used in Western blot analysis.
    Figure Legend Snippet: Antibodies used in Western blot analysis.

    Techniques Used: Western Blot

    synaptotagmin  (Alomone Labs)


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    Structured Review

    Alomone Labs synaptotagmin
    Specific silencing of SNAP-25 by RNA interference . A) Immunoblots were done to assess the levels of SNAP-25, SNAP-23, <t>synaptotagmin</t> I, syntaxin 1A, tyrosine hydroxylase and β-actin in wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells (PC12 cells stably transfected with pG418-shRNA lacking an shRNA insert). Equal amounts of protein were loaded per lane. B) The SNAP-25 phenotype is maintained for at least 10 weeks in culture in both the parent PC12 cell line and the SNAP-25 knockdown cell line. C) Human and zebrafish SNAP-25 mRNAs are resistant to RNA interference. The specificity of the SNAP-25 shRNA was demonstrated by transiently transfecting SNAP-25 knockdown cells with plasmids designed to express SNAP-25 cDNA of rat, human, or zebrafish origin. The 19 nucleotide region of rat SNAP-25 mRNA which is targeted by the SNAP-25 shRNA differs from human SNAP-25 RNA at only 2 positions and from zebrafish SNAP-25 mRNA in 4 positions. The immunoblot shows that expression of rat SNAP-25 was silenced in the SNAP-25 knockdown cells, but human and zebrafish SNAP-25 were expressed. All three SNAP-25 cDNAs appeared to be expressed in the control transfected cells in that there was more SNAP-25 in the control transfected cells than in untransfected PC12 cells. The immunoblot was stripped and reprobed for β-actin to demonstrate approximately equal amounts of protein in each sample. D) SNAP-25 mRNA is reduced in SNAP-25 knockdown cells. RT-PCR was carried out with RNA isolated from wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells. SNAP-25 mRNA was easily detected in wild type and control transfected PC12 cells, but no SNAP-25 mRNA was detected in the SNAP-25 knockdown cells in this PCR experiments. However, if more of the reverse-transcription product was used for the PCR or if more cycles were done in the PCR reaction, some SNAP-25 mRNA was detectable in the SNAP-25 knockdown cells.
    Synaptotagmin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    86/100 stars

    Images

    1) Product Images from "Stable silencing of SNAP-25 in PC12 cells by RNA interference"

    Article Title: Stable silencing of SNAP-25 in PC12 cells by RNA interference

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-7-9

    Specific silencing of SNAP-25 by RNA interference . A) Immunoblots were done to assess the levels of SNAP-25, SNAP-23, synaptotagmin I, syntaxin 1A, tyrosine hydroxylase and β-actin in wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells (PC12 cells stably transfected with pG418-shRNA lacking an shRNA insert). Equal amounts of protein were loaded per lane. B) The SNAP-25 phenotype is maintained for at least 10 weeks in culture in both the parent PC12 cell line and the SNAP-25 knockdown cell line. C) Human and zebrafish SNAP-25 mRNAs are resistant to RNA interference. The specificity of the SNAP-25 shRNA was demonstrated by transiently transfecting SNAP-25 knockdown cells with plasmids designed to express SNAP-25 cDNA of rat, human, or zebrafish origin. The 19 nucleotide region of rat SNAP-25 mRNA which is targeted by the SNAP-25 shRNA differs from human SNAP-25 RNA at only 2 positions and from zebrafish SNAP-25 mRNA in 4 positions. The immunoblot shows that expression of rat SNAP-25 was silenced in the SNAP-25 knockdown cells, but human and zebrafish SNAP-25 were expressed. All three SNAP-25 cDNAs appeared to be expressed in the control transfected cells in that there was more SNAP-25 in the control transfected cells than in untransfected PC12 cells. The immunoblot was stripped and reprobed for β-actin to demonstrate approximately equal amounts of protein in each sample. D) SNAP-25 mRNA is reduced in SNAP-25 knockdown cells. RT-PCR was carried out with RNA isolated from wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells. SNAP-25 mRNA was easily detected in wild type and control transfected PC12 cells, but no SNAP-25 mRNA was detected in the SNAP-25 knockdown cells in this PCR experiments. However, if more of the reverse-transcription product was used for the PCR or if more cycles were done in the PCR reaction, some SNAP-25 mRNA was detectable in the SNAP-25 knockdown cells.
    Figure Legend Snippet: Specific silencing of SNAP-25 by RNA interference . A) Immunoblots were done to assess the levels of SNAP-25, SNAP-23, synaptotagmin I, syntaxin 1A, tyrosine hydroxylase and β-actin in wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells (PC12 cells stably transfected with pG418-shRNA lacking an shRNA insert). Equal amounts of protein were loaded per lane. B) The SNAP-25 phenotype is maintained for at least 10 weeks in culture in both the parent PC12 cell line and the SNAP-25 knockdown cell line. C) Human and zebrafish SNAP-25 mRNAs are resistant to RNA interference. The specificity of the SNAP-25 shRNA was demonstrated by transiently transfecting SNAP-25 knockdown cells with plasmids designed to express SNAP-25 cDNA of rat, human, or zebrafish origin. The 19 nucleotide region of rat SNAP-25 mRNA which is targeted by the SNAP-25 shRNA differs from human SNAP-25 RNA at only 2 positions and from zebrafish SNAP-25 mRNA in 4 positions. The immunoblot shows that expression of rat SNAP-25 was silenced in the SNAP-25 knockdown cells, but human and zebrafish SNAP-25 were expressed. All three SNAP-25 cDNAs appeared to be expressed in the control transfected cells in that there was more SNAP-25 in the control transfected cells than in untransfected PC12 cells. The immunoblot was stripped and reprobed for β-actin to demonstrate approximately equal amounts of protein in each sample. D) SNAP-25 mRNA is reduced in SNAP-25 knockdown cells. RT-PCR was carried out with RNA isolated from wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells. SNAP-25 mRNA was easily detected in wild type and control transfected PC12 cells, but no SNAP-25 mRNA was detected in the SNAP-25 knockdown cells in this PCR experiments. However, if more of the reverse-transcription product was used for the PCR or if more cycles were done in the PCR reaction, some SNAP-25 mRNA was detectable in the SNAP-25 knockdown cells.

    Techniques Used: Western Blot, Transfection, Stable Transfection, shRNA, Expressing, Reverse Transcription Polymerase Chain Reaction, Isolation

    rabbit polyclonal anti syt 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti syt 1
    <t>SYT-1</t> protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.
    Rabbit Polyclonal Anti Syt 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti syt 1/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti syt 1 - by Bioz Stars, 2023-02
    92/100 stars

    Images

    1) Product Images from "An altered glial phenotype in the NL3 R451C mouse model of autism"

    Article Title: An altered glial phenotype in the NL3 R451C mouse model of autism

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-71171-y

    SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.
    Figure Legend Snippet: SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.

    Techniques Used: Expressing, Western Blot, Two Tailed Test

    Antibodies used in Western blot analysis.
    Figure Legend Snippet: Antibodies used in Western blot analysis.

    Techniques Used: Western Blot

    223 anti synaptotagmin 1  (Alomone Labs)


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    Alomone Labs 223 anti synaptotagmin 1
    223 Anti Synaptotagmin 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 1 article reviews
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    223 anti synaptotagmin 1 - by Bioz Stars, 2023-02
    92/100 stars

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    anti p65  (Alomone Labs)


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    Alomone Labs anti p65
    ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with <t>p65</t> siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)
    Anti P65, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p65/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
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    anti p65 - by Bioz Stars, 2023-02
    92/100 stars

    Images

    1) Product Images from "Alpha‐lipoic acid downregulates TRPV1 receptor via NF‐κB and attenuates neuropathic pain in rats with diabetes"

    Article Title: Alpha‐lipoic acid downregulates TRPV1 receptor via NF‐κB and attenuates neuropathic pain in rats with diabetes

    Journal: CNS Neuroscience & Therapeutics

    doi: 10.1111/cns.13303

    ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with p65 siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)
    Figure Legend Snippet: ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with p65 siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)

    Techniques Used: Expressing, Western Blot, Injection

    rabbit polyclonal anti synaptotagmin 1 antibody  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti synaptotagmin 1 antibody
    Rabbit Polyclonal Anti Synaptotagmin 1 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti synaptotagmin 1 antibody/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
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    rabbit polyclonal anti synaptotagmin 1 antibody - by Bioz Stars, 2023-02
    92/100 stars

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    anti p65  (Alomone Labs)


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    Alomone Labs anti p65
    Both expression and phosphorylation of NF-κB subunits in SMA mouse DRGs were increased. L4–L6 DRGs were isolated from SMA and heterozygous (Het) mice at 9 weeks of age. Total 18 DRGs were pooled together for each RNA or protein sample. ( a ) Nfkb1 and Rela mRNA levels were analyzed with qRT-PCR using specific primers and normalized to Gapdh (n = 4 per group). ( b ) Western blotting was used to analyze protein levels of SMN (n = 3), p50 (n = 4), <t>p65</t> (n = 4), p-p50 (n = 3), and p-p65 (n = 4), respectively, in DRGs with specific antibodies. GAPDH was used as a loading control. c Fold changes of protein signals in SMA mice shown in panel (b). For panels (a,c), * P < 0.05, ** P < 0.01, *** P < 0.001 versus Het. ( d – e) DRG sections, derived from five SMA and five Het mice, were stained with anti-p-p50 antibody or anti-p-p65 (green) with NeuN (red) being a neuronal marker. DAPI (blue) was used to stain nuclei. Scale bar, 25 μm. Representative images are shown.
    Anti P65, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p65/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti p65 - by Bioz Stars, 2023-02
    92/100 stars

    Images

    1) Product Images from "SMN deficiency causes pain hypersensitivity in a mild SMA mouse model through enhancing excitability of nociceptive dorsal root ganglion neurons"

    Article Title: SMN deficiency causes pain hypersensitivity in a mild SMA mouse model through enhancing excitability of nociceptive dorsal root ganglion neurons

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-43053-5

    Both expression and phosphorylation of NF-κB subunits in SMA mouse DRGs were increased. L4–L6 DRGs were isolated from SMA and heterozygous (Het) mice at 9 weeks of age. Total 18 DRGs were pooled together for each RNA or protein sample. ( a ) Nfkb1 and Rela mRNA levels were analyzed with qRT-PCR using specific primers and normalized to Gapdh (n = 4 per group). ( b ) Western blotting was used to analyze protein levels of SMN (n = 3), p50 (n = 4), p65 (n = 4), p-p50 (n = 3), and p-p65 (n = 4), respectively, in DRGs with specific antibodies. GAPDH was used as a loading control. c Fold changes of protein signals in SMA mice shown in panel (b). For panels (a,c), * P < 0.05, ** P < 0.01, *** P < 0.001 versus Het. ( d – e) DRG sections, derived from five SMA and five Het mice, were stained with anti-p-p50 antibody or anti-p-p65 (green) with NeuN (red) being a neuronal marker. DAPI (blue) was used to stain nuclei. Scale bar, 25 μm. Representative images are shown.
    Figure Legend Snippet: Both expression and phosphorylation of NF-κB subunits in SMA mouse DRGs were increased. L4–L6 DRGs were isolated from SMA and heterozygous (Het) mice at 9 weeks of age. Total 18 DRGs were pooled together for each RNA or protein sample. ( a ) Nfkb1 and Rela mRNA levels were analyzed with qRT-PCR using specific primers and normalized to Gapdh (n = 4 per group). ( b ) Western blotting was used to analyze protein levels of SMN (n = 3), p50 (n = 4), p65 (n = 4), p-p50 (n = 3), and p-p65 (n = 4), respectively, in DRGs with specific antibodies. GAPDH was used as a loading control. c Fold changes of protein signals in SMA mice shown in panel (b). For panels (a,c), * P < 0.05, ** P < 0.01, *** P < 0.001 versus Het. ( d – e) DRG sections, derived from five SMA and five Het mice, were stained with anti-p-p50 antibody or anti-p-p65 (green) with NeuN (red) being a neuronal marker. DAPI (blue) was used to stain nuclei. Scale bar, 25 μm. Representative images are shown.

    Techniques Used: Expressing, Isolation, Quantitative RT-PCR, Western Blot, Derivative Assay, Staining, Marker

    Elevated plasma NE levels in SMA mice enhance expression and phosphorylation of NF-κB subunits in DRGs. ( a , b ) Plasma E (n = 4) and NE (n = 10) concentrations in SMA and Het mice aged 3 or 9 weeks were measured with Elisa kits. ( c , d ) Mice at 9 weeks old were intraperitoneally injected with 1 mg/kg/day prop for seven consecutive days and then L4–L6 DRG RNA and protein samples were isolated for qRT-PCR analysis of expression of Scn9a , Scn10a , Nfkb1 and Rela with specific primers and normalization to Gapdh (n = 3), or for western blotting analysis with specific antibodies against p50, p65, p-p50, p-p65, Na v 1.7 and Na v 1.8 (n = 3–4), respectively; GAPDH was used as a loading control. ( e) Quantitation of data in panel (d), presented as fold changes. ( f – g ) NE was intraperitoneally injected into 9 weeks old mice at indicated doses (ng/g), and 30 min post injection mechanical sensitivity was assessed with von Frey test. Mechanical withdraw threshold (MWT) was recorded for each mouse. For all panels, * P < 0.05, ** P < 0.01, *** P < 0.01 and # P > 0.05 versus Het or saline treatment.
    Figure Legend Snippet: Elevated plasma NE levels in SMA mice enhance expression and phosphorylation of NF-κB subunits in DRGs. ( a , b ) Plasma E (n = 4) and NE (n = 10) concentrations in SMA and Het mice aged 3 or 9 weeks were measured with Elisa kits. ( c , d ) Mice at 9 weeks old were intraperitoneally injected with 1 mg/kg/day prop for seven consecutive days and then L4–L6 DRG RNA and protein samples were isolated for qRT-PCR analysis of expression of Scn9a , Scn10a , Nfkb1 and Rela with specific primers and normalization to Gapdh (n = 3), or for western blotting analysis with specific antibodies against p50, p65, p-p50, p-p65, Na v 1.7 and Na v 1.8 (n = 3–4), respectively; GAPDH was used as a loading control. ( e) Quantitation of data in panel (d), presented as fold changes. ( f – g ) NE was intraperitoneally injected into 9 weeks old mice at indicated doses (ng/g), and 30 min post injection mechanical sensitivity was assessed with von Frey test. Mechanical withdraw threshold (MWT) was recorded for each mouse. For all panels, * P < 0.05, ** P < 0.01, *** P < 0.01 and # P > 0.05 versus Het or saline treatment.

    Techniques Used: Expressing, Enzyme-linked Immunosorbent Assay, Injection, Isolation, Quantitative RT-PCR, Western Blot, Quantitation Assay

    A model depicting a molecular mechanism underlying pain hypersensitivity in mild SMA mice. SMN deficiency leads to autonomic dysfunction that causes increased release of NE, which in turn, mediated by ADRB/β2AR, enhances NF-κB signaling in nociceptive DRG neurons through increasing expression and phosphorylation of p50 and p65. Enhanced NF-κB activity promotes expression of Na v 1.7 and Na v 1.8, contributing to hyperexcitability of these DRG neurons and pain hypersensitivity in SMA mice.
    Figure Legend Snippet: A model depicting a molecular mechanism underlying pain hypersensitivity in mild SMA mice. SMN deficiency leads to autonomic dysfunction that causes increased release of NE, which in turn, mediated by ADRB/β2AR, enhances NF-κB signaling in nociceptive DRG neurons through increasing expression and phosphorylation of p50 and p65. Enhanced NF-κB activity promotes expression of Na v 1.7 and Na v 1.8, contributing to hyperexcitability of these DRG neurons and pain hypersensitivity in SMA mice.

    Techniques Used: Expressing, Activity Assay

    synaptotagmin  (Alomone Labs)


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    Alomone Labs synaptotagmin
    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the <t>synaptotagmin+</t> “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Synaptotagmin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/synaptotagmin/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    synaptotagmin - by Bioz Stars, 2023-02
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    1) Product Images from "WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity"

    Article Title: WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0328-18.2018

    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Figure Legend Snippet: WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.

    Techniques Used: Expressing, Injection, Staining, Labeling, Marker

    synaptotagmin  (Alomone Labs)


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    Alomone Labs synaptotagmin
    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the <t>synaptotagmin+</t> “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Synaptotagmin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity"

    Article Title: WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0328-18.2018

    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Figure Legend Snippet: WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.

    Techniques Used: Expressing, Injection, Staining, Labeling, Marker

    synaptotagmin  (Alomone Labs)


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    Alomone Labs synaptotagmin
    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the <t>synaptotagmin+</t> “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Synaptotagmin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/synaptotagmin/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
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    synaptotagmin - by Bioz Stars, 2023-02
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    Images

    1) Product Images from "WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity"

    Article Title: WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0328-18.2018

    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Figure Legend Snippet: WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.

    Techniques Used: Expressing, Injection, Staining, Labeling, Marker

    synaptotagmin  (Alomone Labs)


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    Alomone Labs synaptotagmin
    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the <t>synaptotagmin+</t> “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Synaptotagmin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/synaptotagmin/product/Alomone Labs
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    Images

    1) Product Images from "WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity"

    Article Title: WT1 -Expressing Interneurons Regulate Left–Right Alternation during Mammalian Locomotor Activity

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0328-18.2018

    WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.
    Figure Legend Snippet: WT1-expressing neurons terminate in close proximity to populations of commissurally projecting interneurons. A, A 20-μm-thick section of a spinal cord 46 h after PRV-152 injection into the GS muscle on the left side and stained with antibodies to GFP (green) and WT1 (blue). At this time point, no WT1-expressing neurons on either side of the spinal cord have taken up the tracer. Contralateral region containing WT1-expressing cells (dashed box) is expanded to the right. B, To identify presumptive synapses on genetically defined interneuronal subtypes, we inspected the synaptotagmin+ “halo” (indicated by white arrows) surrounding each labeled nuclei for WT1+/synaptotagmin+ terminals. C–F, The 20-μm-thick sections cut from a P0 WT1CreERROSA26tdTomato spinal cord and stained with antibodies to tdTomato (red), the synaptic marker synatotagmin (blue), as well as (green) a nuclear marker of V2a cells (Chx10-, C), V1 cells (En1-, D), V0V cells (Evx1-, E), or DMRT3-expressing dI6 cells (F). WT1-expressing terminals (tdTomato+/synaptotagmin+ processes) were rare or absent nearby Chx10- or En1-expressing cells but were commonly seen in close proximity to Evx1+ and DMRT3+ neurons. C, D, Dashed boxes are expanded to the right. E, F, Arrow in the low-magnification image indicates the specific WT1 cell of interest in the panel to the right. In magnified images, arrows indicate presumptive WT1+ axon terminals. Double labeling of these processes is confirmed in orthogonal views to the right of E, F. Scale bars: Low-magnification images, 100 μm; High-magnification images: A, C, D, 20 μm; B, E, F, 5 μm.

    Techniques Used: Expressing, Injection, Staining, Labeling, Marker

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    Alomone Labs rabbit polyclonal anti synaptotagmin 1 antibody
    ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with <t>p65</t> siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)
    Rabbit Polyclonal Anti Synaptotagmin 1 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal anti synaptotagmin 1 antibody - by Bioz Stars, 2023-02
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    SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.

    Journal: Scientific Reports

    Article Title: An altered glial phenotype in the NL3 R451C mouse model of autism

    doi: 10.1038/s41598-020-71171-y

    Figure Lengend Snippet: SYT-1 protein levels are unchanged, but SNAP-25 protein expression was decreased in the cortex of NL3 R451C mice. SYT-1 and SNAP-25 protein expression in cortical ( A , G ), striatal ( C , I ) and cerebellar ( E , K ) lysates from NL3 R451C and WT mice were analysed via Western blot. Densitometric analysis was performed to demonstrate quantitative expression of SYT-1 ( B ,D, F ) and SNAP-25 ( H , J , L ) relative to β actin expression. Genotype differences were analysed using an unpaired, two-tailed Student’s t-test (n = 6 mice in each group); **p < 0.01. Data represented as mean ± SEM.

    Article Snippet: Rabbit polyclonal anti-SYT-1 (48 kDa) , Alomone Labs #ANR-003 , 1:500.

    Techniques: Expressing, Western Blot, Two Tailed Test

    Antibodies used in Western blot analysis.

    Journal: Scientific Reports

    Article Title: An altered glial phenotype in the NL3 R451C mouse model of autism

    doi: 10.1038/s41598-020-71171-y

    Figure Lengend Snippet: Antibodies used in Western blot analysis.

    Article Snippet: Rabbit polyclonal anti-SYT-1 (48 kDa) , Alomone Labs #ANR-003 , 1:500.

    Techniques: Western Blot

    Specific silencing of SNAP-25 by RNA interference . A) Immunoblots were done to assess the levels of SNAP-25, SNAP-23, synaptotagmin I, syntaxin 1A, tyrosine hydroxylase and β-actin in wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells (PC12 cells stably transfected with pG418-shRNA lacking an shRNA insert). Equal amounts of protein were loaded per lane. B) The SNAP-25 phenotype is maintained for at least 10 weeks in culture in both the parent PC12 cell line and the SNAP-25 knockdown cell line. C) Human and zebrafish SNAP-25 mRNAs are resistant to RNA interference. The specificity of the SNAP-25 shRNA was demonstrated by transiently transfecting SNAP-25 knockdown cells with plasmids designed to express SNAP-25 cDNA of rat, human, or zebrafish origin. The 19 nucleotide region of rat SNAP-25 mRNA which is targeted by the SNAP-25 shRNA differs from human SNAP-25 RNA at only 2 positions and from zebrafish SNAP-25 mRNA in 4 positions. The immunoblot shows that expression of rat SNAP-25 was silenced in the SNAP-25 knockdown cells, but human and zebrafish SNAP-25 were expressed. All three SNAP-25 cDNAs appeared to be expressed in the control transfected cells in that there was more SNAP-25 in the control transfected cells than in untransfected PC12 cells. The immunoblot was stripped and reprobed for β-actin to demonstrate approximately equal amounts of protein in each sample. D) SNAP-25 mRNA is reduced in SNAP-25 knockdown cells. RT-PCR was carried out with RNA isolated from wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells. SNAP-25 mRNA was easily detected in wild type and control transfected PC12 cells, but no SNAP-25 mRNA was detected in the SNAP-25 knockdown cells in this PCR experiments. However, if more of the reverse-transcription product was used for the PCR or if more cycles were done in the PCR reaction, some SNAP-25 mRNA was detectable in the SNAP-25 knockdown cells.

    Journal: BMC Neuroscience

    Article Title: Stable silencing of SNAP-25 in PC12 cells by RNA interference

    doi: 10.1186/1471-2202-7-9

    Figure Lengend Snippet: Specific silencing of SNAP-25 by RNA interference . A) Immunoblots were done to assess the levels of SNAP-25, SNAP-23, synaptotagmin I, syntaxin 1A, tyrosine hydroxylase and β-actin in wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells (PC12 cells stably transfected with pG418-shRNA lacking an shRNA insert). Equal amounts of protein were loaded per lane. B) The SNAP-25 phenotype is maintained for at least 10 weeks in culture in both the parent PC12 cell line and the SNAP-25 knockdown cell line. C) Human and zebrafish SNAP-25 mRNAs are resistant to RNA interference. The specificity of the SNAP-25 shRNA was demonstrated by transiently transfecting SNAP-25 knockdown cells with plasmids designed to express SNAP-25 cDNA of rat, human, or zebrafish origin. The 19 nucleotide region of rat SNAP-25 mRNA which is targeted by the SNAP-25 shRNA differs from human SNAP-25 RNA at only 2 positions and from zebrafish SNAP-25 mRNA in 4 positions. The immunoblot shows that expression of rat SNAP-25 was silenced in the SNAP-25 knockdown cells, but human and zebrafish SNAP-25 were expressed. All three SNAP-25 cDNAs appeared to be expressed in the control transfected cells in that there was more SNAP-25 in the control transfected cells than in untransfected PC12 cells. The immunoblot was stripped and reprobed for β-actin to demonstrate approximately equal amounts of protein in each sample. D) SNAP-25 mRNA is reduced in SNAP-25 knockdown cells. RT-PCR was carried out with RNA isolated from wild type PC12 cells, SNAP-25 knockdown cells and in control transfected cells. SNAP-25 mRNA was easily detected in wild type and control transfected PC12 cells, but no SNAP-25 mRNA was detected in the SNAP-25 knockdown cells in this PCR experiments. However, if more of the reverse-transcription product was used for the PCR or if more cycles were done in the PCR reaction, some SNAP-25 mRNA was detectable in the SNAP-25 knockdown cells.

    Article Snippet: Levels of SNAP-25, SNAP-23, syntaxin 1A, synaptotagmin I, tyrosine hydroxylase and β-actin in the cell lines were assessed by immunoblotting with the following antibodies: SNAP-25 (ANR-001, Alomone), SNAP-23 (DS-19; Sigma), syntaxin 1A (#573831, Calbiochem), synaptotagmin I (mAb48; Developmental Systems Hybridoma Bank, University of Iowa), tyrosine hydroxylase (#657010, Calbiochem), β-actin (JLA20; Developmental Systems Hybridoma Bank, University of Iowa), and horseradish peroxidase-labeled anti-mouse or anti-rabbit IgG (Jackson ImmunoResearch).

    Techniques: Western Blot, Transfection, Stable Transfection, shRNA, Expressing, Reverse Transcription Polymerase Chain Reaction, Isolation

    ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with p65 siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)

    Journal: CNS Neuroscience & Therapeutics

    Article Title: Alpha‐lipoic acid downregulates TRPV1 receptor via NF‐κB and attenuates neuropathic pain in rats with diabetes

    doi: 10.1111/cns.13303

    Figure Lengend Snippet: ALA inhibited TRPV1 expression via suppressing NF‐κB. A, Western blots for NF‐κB in DRGs innervating the hindpaw from control and STZ‐induced diabetic rats. Bar graph involved mean density relative of β‐actin and NF‐κB from control and STZ‐induced diabetic rats. STZ injection significantly enhanced expression of NF‐κB (N = 4 for each group; * P < .05, compared with CNT, two‐sample t test) in L4‐L6 DRGs. B, Western blots for TRPV1 in L4‐L6 DRGs from diabetic rats treated with p65 siRNA lentivirus and NC siRNA lentivirus, respectively. Graph showed mean density relative to GAPDH for TRPV1. The lentiviruses were intrathecally injected into rats. The expression of TRPV1 significantly reduced after p65 siRNA lentiviruses treatment compared with NC siRNA group (N = 4 for each group, * P < .05, compared with NC siR, two‐sample t test). C, Western blots for NF‐κB in L4‐L6 DRGs from diabetic rats treated with NS and ALA, respectively. Graph showed mean density relative to GAPDH for NF‐κB. ALA treatment strongly reduced the expression of NF‐κB (N = 4 for NS group, N = 3 for ALA group, ** P < .01, compared with NS, two‐sample t test)

    Article Snippet: Anti‐TRPV1 (#ACC‐030, Alomone, 1:200), anti‐p65 (#6956, Cell Signaling Technology, 1:1000), and corresponding horseradish peroxidase‐conjugated secondary anti‐rabbit and anti‐mouse antibodies at dilutions of 1:2000 and 1:2000 were used to probe the proteins, respectively.

    Techniques: Expressing, Western Blot, Injection