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stat3 specific antibody h 190 (Santa Cruz Biotechnology)

Name: stat3 specific antibody h 190
Brand: Santa Cruz Biotechnology
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Santa Cruz Biotechnology stat3 specific antibody h 190

(A, B) Gelshift experiments demonstrated that STAT1-T385A and wild-type protein exhibit a similar dissociation rate from a single STAT1-binding site (M67). Cell lysates from IFNγ-stimulated U3A cells (5 ng/ml) expressing either wild-type or mutant STAT1 were incubated with [ 33 P]-labeled M67 for 15 min and subsequently a 750-fold molar excess of unlabeled M67 was added for the durations indicated, before the reactions were loaded onto a native polyacrylamide gel. Shown is a typical gel, with the arrowhead at its right-hand margin corresponding to dimeric STAT1, including a densitometric quantification thereof. Asterisks mark unspecific bands. (C) The T385A mutant displays cooperative DNA binding due to tetramer stabilization. Extracts from an equal number of IFNγ-stimulated U3A cells expressing either wild-type or mutant STAT1 (5 µl in each lane) were incubated in vitro with [ 33 P]-labeled DNA containing two GAS sites separated by 10 bp (2xGAS). The reactions were either left unchallenged (−) or challenged for 30 min with a 750-fold excess of a single, unlabeled GAS site (+ Competition). Note that the tetrameric, but not the dimeric occupancy of the probe resisted competition with excess unlabeled DNA. (D) Gelshift experiments demonstrate the propensity of tetrameric STAT1-T385A to exchange dimers. Shown is a representative gel using [ 33 P]-labeled 2xGAS and cellular extracts from IFNγ/vanadate-co-stimulated U3A cells expressing either GFP-tagged or untagged STAT1. Supershifts with either <t>anti-STAT3</t> (lane 1 and 3) or anti-STAT1 (lane 2 and 4) antibodies identified bands corresponding to DNA-bound STAT1. For the identification of dimeric STAT1 complexes, a competition experiment using 750-molar excess of unlabelled GAS was included in the last lane. Similar amounts of GFP-tagged and untagged homodimers were either immediately mixed and incubated together for 45 min (lanes 6 and 8) or incubated separately for 45 min before being loaded together onto the gel (lanes 5 and 7). Note that newly formed bands corresponding to STAT-GFP/STAT1 heterotetramers appeared only in extracts that had been co-incubated. (E) The T385A mutant binds to GAS sequences as a tetramer. Whole cell extracts from reconstituted, IFNγ-prestimulated U3A cells were incubated with various [ 33 P]-labeled DNA probes containing either two (2xGAS), one (GAS-nonGAS) or no (2xnonGAS) GAS sites, respectively. In the first lane, a non-specific anti-STAT3 antibody and in the second lane, anti-STAT1 antibody C-24 was present in the EMSA reaction used for identification of STAT1-DNA complexes (marked with arrowheads). (F) The F172W and T385A mutants are defective in tyrosine dephosphorylation as revealed by an in vitro dephosphorylation assay using purified Tc45 phosphatase. Cell extracts from reconstituted U3A cells expressing either wild-type or mutant STAT1 (10 µl in each reaction) were incubated with 2 U of the STAT1-specific Tc45 phosphatase and tyrosine dephosphorylation was monitored with time by means of Western blotting.

Stat3 Specific Antibody H 190, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 4569 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Clinically Relevant Dimer Interface Mutants of STAT1 Transcription Factor Exhibit Differential Gene Expression"

Article Title: Clinically Relevant Dimer Interface Mutants of STAT1 Transcription Factor Exhibit Differential Gene Expression

Journal: PLoS ONE

doi: 10.1371/journal.pone.0069903

Figure Legend Snippet: (A, B) Gelshift experiments demonstrated that STAT1-T385A and wild-type protein exhibit a similar dissociation rate from a single STAT1-binding site (M67). Cell lysates from IFNγ-stimulated U3A cells (5 ng/ml) expressing either wild-type or mutant STAT1 were incubated with [ 33 P]-labeled M67 for 15 min and subsequently a 750-fold molar excess of unlabeled M67 was added for the durations indicated, before the reactions were loaded onto a native polyacrylamide gel. Shown is a typical gel, with the arrowhead at its right-hand margin corresponding to dimeric STAT1, including a densitometric quantification thereof. Asterisks mark unspecific bands. (C) The T385A mutant displays cooperative DNA binding due to tetramer stabilization. Extracts from an equal number of IFNγ-stimulated U3A cells expressing either wild-type or mutant STAT1 (5 µl in each lane) were incubated in vitro with [ 33 P]-labeled DNA containing two GAS sites separated by 10 bp (2xGAS). The reactions were either left unchallenged (−) or challenged for 30 min with a 750-fold excess of a single, unlabeled GAS site (+ Competition). Note that the tetrameric, but not the dimeric occupancy of the probe resisted competition with excess unlabeled DNA. (D) Gelshift experiments demonstrate the propensity of tetrameric STAT1-T385A to exchange dimers. Shown is a representative gel using [ 33 P]-labeled 2xGAS and cellular extracts from IFNγ/vanadate-co-stimulated U3A cells expressing either GFP-tagged or untagged STAT1. Supershifts with either anti-STAT3 (lane 1 and 3) or anti-STAT1 (lane 2 and 4) antibodies identified bands corresponding to DNA-bound STAT1. For the identification of dimeric STAT1 complexes, a competition experiment using 750-molar excess of unlabelled GAS was included in the last lane. Similar amounts of GFP-tagged and untagged homodimers were either immediately mixed and incubated together for 45 min (lanes 6 and 8) or incubated separately for 45 min before being loaded together onto the gel (lanes 5 and 7). Note that newly formed bands corresponding to STAT-GFP/STAT1 heterotetramers appeared only in extracts that had been co-incubated. (E) The T385A mutant binds to GAS sequences as a tetramer. Whole cell extracts from reconstituted, IFNγ-prestimulated U3A cells were incubated with various [ 33 P]-labeled DNA probes containing either two (2xGAS), one (GAS-nonGAS) or no (2xnonGAS) GAS sites, respectively. In the first lane, a non-specific anti-STAT3 antibody and in the second lane, anti-STAT1 antibody C-24 was present in the EMSA reaction used for identification of STAT1-DNA complexes (marked with arrowheads). (F) The F172W and T385A mutants are defective in tyrosine dephosphorylation as revealed by an in vitro dephosphorylation assay using purified Tc45 phosphatase. Cell extracts from reconstituted U3A cells expressing either wild-type or mutant STAT1 (10 µl in each reaction) were incubated with 2 U of the STAT1-specific Tc45 phosphatase and tyrosine dephosphorylation was monitored with time by means of Western blotting.

Techniques Used: Binding Assay, Expressing, Mutagenesis, Incubation, Labeling, In Vitro, De-Phosphorylation Assay, Purification, Western Blot

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Journal: PLoS ONE

Article Title: Clinically Relevant Dimer Interface Mutants of STAT1 Transcription Factor Exhibit Differential Gene Expression

doi: 10.1371/journal.pone.0069903

Figure Lengend Snippet: (A, B) Gelshift experiments demonstrated that STAT1-T385A and wild-type protein exhibit a similar dissociation rate from a single STAT1-binding site (M67). Cell lysates from IFNγ-stimulated U3A cells (5 ng/ml) expressing either wild-type or mutant STAT1 were incubated with [ 33 P]-labeled M67 for 15 min and subsequently a 750-fold molar excess of unlabeled M67 was added for the durations indicated, before the reactions were loaded onto a native polyacrylamide gel. Shown is a typical gel, with the arrowhead at its right-hand margin corresponding to dimeric STAT1, including a densitometric quantification thereof. Asterisks mark unspecific bands. (C) The T385A mutant displays cooperative DNA binding due to tetramer stabilization. Extracts from an equal number of IFNγ-stimulated U3A cells expressing either wild-type or mutant STAT1 (5 µl in each lane) were incubated in vitro with [ 33 P]-labeled DNA containing two GAS sites separated by 10 bp (2xGAS). The reactions were either left unchallenged (−) or challenged for 30 min with a 750-fold excess of a single, unlabeled GAS site (+ Competition). Note that the tetrameric, but not the dimeric occupancy of the probe resisted competition with excess unlabeled DNA. (D) Gelshift experiments demonstrate the propensity of tetrameric STAT1-T385A to exchange dimers. Shown is a representative gel using [ 33 P]-labeled 2xGAS and cellular extracts from IFNγ/vanadate-co-stimulated U3A cells expressing either GFP-tagged or untagged STAT1. Supershifts with either anti-STAT3 (lane 1 and 3) or anti-STAT1 (lane 2 and 4) antibodies identified bands corresponding to DNA-bound STAT1. For the identification of dimeric STAT1 complexes, a competition experiment using 750-molar excess of unlabelled GAS was included in the last lane. Similar amounts of GFP-tagged and untagged homodimers were either immediately mixed and incubated together for 45 min (lanes 6 and 8) or incubated separately for 45 min before being loaded together onto the gel (lanes 5 and 7). Note that newly formed bands corresponding to STAT-GFP/STAT1 heterotetramers appeared only in extracts that had been co-incubated. (E) The T385A mutant binds to GAS sequences as a tetramer. Whole cell extracts from reconstituted, IFNγ-prestimulated U3A cells were incubated with various [ 33 P]-labeled DNA probes containing either two (2xGAS), one (GAS-nonGAS) or no (2xnonGAS) GAS sites, respectively. In the first lane, a non-specific anti-STAT3 antibody and in the second lane, anti-STAT1 antibody C-24 was present in the EMSA reaction used for identification of STAT1-DNA complexes (marked with arrowheads). (F) The F172W and T385A mutants are defective in tyrosine dephosphorylation as revealed by an in vitro dephosphorylation assay using purified Tc45 phosphatase. Cell extracts from reconstituted U3A cells expressing either wild-type or mutant STAT1 (10 µl in each reaction) were incubated with 2 U of the STAT1-specific Tc45 phosphatase and tyrosine dephosphorylation was monitored with time by means of Western blotting.

Article Snippet: In supershift reactions, 20 ng of the STAT1-specific antibody C-24 or the STAT3-specific antibody H-190 (both from Santa Cruz Biotechnology) were preincubated with the shift reactions for 20 min at RT.

Techniques: Binding Assay, Expressing, Mutagenesis, Incubation, Labeling, In Vitro, De-Phosphorylation Assay, Purification, Western Blot

(A & C): The effect of IGF-1R suppression on ERK and STAT signaling was examined in pancreatic cancer cells. Whole cell lysates were separated by SDS-PAGE and analyzed by Western blot for expression levels of phospho-ERK, ERK, IR-β, phospho-IRS-1, IRS, phospho-STAT3, STAT3, COX-2 and β-actin. (B & D): Representative blots are presented and corresponding densitometric analysis is shown to the right of each image. PS-PANC-1 Scrambled, PI-PANC-1 IGF-1R silenced, HS-HPAC Scrambled, HI-HPAC IGF-1R silenced.

Journal: PLoS ONE

Article Title: Targeting Insulin-Like Growth Factor 1 Receptor Inhibits Pancreatic Cancer Growth and Metastasis

doi: 10.1371/journal.pone.0097016

Figure Lengend Snippet: (A & C): The effect of IGF-1R suppression on ERK and STAT signaling was examined in pancreatic cancer cells. Whole cell lysates were separated by SDS-PAGE and analyzed by Western blot for expression levels of phospho-ERK, ERK, IR-β, phospho-IRS-1, IRS, phospho-STAT3, STAT3, COX-2 and β-actin. (B & D): Representative blots are presented and corresponding densitometric analysis is shown to the right of each image. PS-PANC-1 Scrambled, PI-PANC-1 IGF-1R silenced, HS-HPAC Scrambled, HI-HPAC IGF-1R silenced.

Article Snippet: The following primary antibodies were used in this study: pAKT(sc-101629), AKT(5298), Bcl-2(sc-783), pERK, (sc-101760), ERK (sc-94) and STAT3(H-190)(sc-7179) (Santa Cruz,CA,USA); IGF-1R(3027), Notch 2 (4530P), Snail (3879), E-cadherin (3195), N-cadherin (4061), Zeb (3396), Vimentin (5741), Slug (9585), Bax (2772), Caspase3 (9661), PARP (9542), pPI3K p85(4228), PI3K p85(4292), IR-β (3024), pIRS-1(2388), IRS-1(2382), pSTAT3 (ser727) (4113), COX-2 (4842), pPTEN (9549), pmTOR (2974), mTOR(4517), p-p70s6kinase (9206) and p70s6kinase (9202) (Cell Signaling Technology, (Boston, MA); Caspase8 (ab 25901) (Abcam, Cambridge, MA, USA); β-actin (Sigma Aldrich, (St.Louis, MO, USA).

Techniques: SDS Page, Western Blot, Expressing

PVT1 promotes glioma progression depending on TRIM24 (A) Re-expression of TRIM24 after PVT1 deletion in U251 cells restores cell proliferation. (B) Knockout of TRIM24 after overexpression of PVT1 in LN229 cells impairs cell proliferation. (C and D) Re-expression of TRIM24 after PVT1 deletion in U251 cells restores colony formation ability. (E and F) Knockout of TRIM24 after overexpression of PVT1 in LN229 cells impaired colony formation ability. Scale bars, 10 mm. (G and H) Representative bioluminescence images and H&E-stained images of xenografts' brains with indicated U251 cells stably transfected with PVT1 sh or TRIM24OE. Scale bars, 2 mm. n = 5. (I) WB analysis of the expression of p-STAT3 after transfection with PVT1 sh or TRIM24OE in U251 and LN229 cells. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

Journal: Molecular Therapy. Nucleic Acids

Article Title: LncRNA PVT1 promotes tumorigenesis of glioblastoma by recruiting COPS5 to deubiquitinate and stabilize TRIM24

doi: 10.1016/j.omtn.2021.11.012

Figure Lengend Snippet: PVT1 promotes glioma progression depending on TRIM24 (A) Re-expression of TRIM24 after PVT1 deletion in U251 cells restores cell proliferation. (B) Knockout of TRIM24 after overexpression of PVT1 in LN229 cells impairs cell proliferation. (C and D) Re-expression of TRIM24 after PVT1 deletion in U251 cells restores colony formation ability. (E and F) Knockout of TRIM24 after overexpression of PVT1 in LN229 cells impaired colony formation ability. Scale bars, 10 mm. (G and H) Representative bioluminescence images and H&E-stained images of xenografts' brains with indicated U251 cells stably transfected with PVT1 sh or TRIM24OE. Scale bars, 2 mm. n = 5. (I) WB analysis of the expression of p-STAT3 after transfection with PVT1 sh or TRIM24OE in U251 and LN229 cells. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

Article Snippet: The antibodies used for western blotting were FLAG (no. F3165, Sigma Aldrich), HA (no. 66006-1-Ig, Proteintech), MYC (no. 2276, Cell Signaling Technology), His (no. 2365, Cell Signaling Technology), β-actin (no. 66009-1-Ig, Proteintech), TRIM24 (no. 14208-1-AP, Proteintech), COPS5 (no. SC-13157, Santa Cruz Biotechnology), STAT3 (H-190) (no. SC-7179, Santa Cruz Biotechnology), and phospho-STAT3 (Y705) (D3A7) (no. 9145, Cell Signaling Technology).

Techniques: Expressing, Knock-Out, Over Expression, Staining, Stable Transfection, Transfection

The TRIM24/ PVT1 /COPS5 complex promotes glioma progression through activating STAT3 pathway (A–D) Effects of overexpression of COPS5 and knockdown of PVT1 or knockout of TRIM24 on cell proliferation (A and B) and colony formation ability (C and D). Scale bars, 10 mm (in U251 and U373 cells compared with control). (E and F) Representative bioluminescence images and H&E-stained images of xenografts' brains with indicated U251 cells stably transfected with COPS5OE, PVT1 sh, or TRIM24sg. Scale bars, 2 mm. n = 5. (G) WB analysis of the expression of p-STAT3 after overexpression of COPS5 and knockdown of PVT1 or knockout of TRIM24 in U251 and U373 cells. (H) Schematic model illustrates the mechanism by which PVT1 recruits COPS5 to deubiquitinate and stabilize TRIM24 so as to promote tumorigenesis of GBM. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

Journal: Molecular Therapy. Nucleic Acids

Article Title: LncRNA PVT1 promotes tumorigenesis of glioblastoma by recruiting COPS5 to deubiquitinate and stabilize TRIM24

doi: 10.1016/j.omtn.2021.11.012

Figure Lengend Snippet: The TRIM24/ PVT1 /COPS5 complex promotes glioma progression through activating STAT3 pathway (A–D) Effects of overexpression of COPS5 and knockdown of PVT1 or knockout of TRIM24 on cell proliferation (A and B) and colony formation ability (C and D). Scale bars, 10 mm (in U251 and U373 cells compared with control). (E and F) Representative bioluminescence images and H&E-stained images of xenografts' brains with indicated U251 cells stably transfected with COPS5OE, PVT1 sh, or TRIM24sg. Scale bars, 2 mm. n = 5. (G) WB analysis of the expression of p-STAT3 after overexpression of COPS5 and knockdown of PVT1 or knockout of TRIM24 in U251 and U373 cells. (H) Schematic model illustrates the mechanism by which PVT1 recruits COPS5 to deubiquitinate and stabilize TRIM24 so as to promote tumorigenesis of GBM. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.

Techniques: Over Expression, Knockdown, Knock-Out, Control, Staining, Stable Transfection, Transfection, Expressing

Influence of NiV-N on the STAT nuclear import system. (A) The associations between STAT1 and Impα5, Impα6, and Impα7 in the presence of N protein were evaluated by immunoprecipitation (IP). The myc-tagged importins were precipitated with an anti-myc antibody, and the coprecipitation of pSTAT1 with Impα5, Impα6, or Impα7 was evaluated in the presence or absence of N protein. A myc-tagged Impα1 construct was employed as a negative control. P protein served as a positive-control antagonist of the interaction between Impα5 and STAT1. (B) The interaction between NiV-N and HA-Impβ1 or HA-Ran was investigated with immunoprecipitation assays using anti-HA and anti-NiV-N antibodies. The myc-Impα5, myc-Impβ1, and NiV-P proteins were included as positive controls for immunoprecipitation. (C) 293T cells were transfected with pCAGGS-NiV-N (encoding a C-terminal HA tag). After 24 h, the cells were treated with 1,000 U/ml IFN-α for 30 min, and immunoprecipitation was conducted using anti-HA antibody. STAT1, STAT2, STAT3, and N protein in the lysates were detected with anti-STAT1 (E-23), -2 (C-20), and -3 (H-190) and anti-N protein antibodies, respectively. The P protein served as a positive control for an N-binding protein. For panels A to C, the experiments were independently repeated three times, and representative blots are displayed. (D) A reporter assay was conducted using 293T cells transfected with the NiV-N or N-S451A plasmid. The expression levels of each N protein and GAPDH are shown. Error bars indicate standard deviations. n.s., not significant. N-S451A-expressing Cos7 cells were treated with 2,000 U/ml of IFN-α. N-S451A and STAT1 were detected with specific antibodies and are shown as z-stack immunofluorescence images. Arrowheads and arrows indicate an N-S451A-expressing and a non-N-S451A-expressing cell, respectively. The experiment was independently conducted three times. (E) The expression plasmids for NiV-N and EGFP-Kir/Gem-W268G (referred to here as rKir/Gem) were transfected into Cos7 cells, and NiV-N was detected with an anti-NiV-N polyclonal antibody. The nuclei were stained with Hoechst dye. Images shown are z-stack data. The arrowheads and arrows point to a NiV-N-expressing and a non-NiV-N-expressing cell, respectively. The bar graph indicates the statistical evaluation of the rKir/Gem distribution. The scores were determined by counting approximately 60 cells from five randomly selected fields. n.s., not significant.

Journal: Journal of Virology

Article Title: Nipah and Hendra Virus Nucleoproteins Inhibit Nuclear Accumulation of Signal Transducer and Activator of Transcription 1 (STAT1) and STAT2 by Interfering with Their Complex Formation

doi: 10.1128/JVI.01136-17

Figure Lengend Snippet: Influence of NiV-N on the STAT nuclear import system. (A) The associations between STAT1 and Impα5, Impα6, and Impα7 in the presence of N protein were evaluated by immunoprecipitation (IP). The myc-tagged importins were precipitated with an anti-myc antibody, and the coprecipitation of pSTAT1 with Impα5, Impα6, or Impα7 was evaluated in the presence or absence of N protein. A myc-tagged Impα1 construct was employed as a negative control. P protein served as a positive-control antagonist of the interaction between Impα5 and STAT1. (B) The interaction between NiV-N and HA-Impβ1 or HA-Ran was investigated with immunoprecipitation assays using anti-HA and anti-NiV-N antibodies. The myc-Impα5, myc-Impβ1, and NiV-P proteins were included as positive controls for immunoprecipitation. (C) 293T cells were transfected with pCAGGS-NiV-N (encoding a C-terminal HA tag). After 24 h, the cells were treated with 1,000 U/ml IFN-α for 30 min, and immunoprecipitation was conducted using anti-HA antibody. STAT1, STAT2, STAT3, and N protein in the lysates were detected with anti-STAT1 (E-23), -2 (C-20), and -3 (H-190) and anti-N protein antibodies, respectively. The P protein served as a positive control for an N-binding protein. For panels A to C, the experiments were independently repeated three times, and representative blots are displayed. (D) A reporter assay was conducted using 293T cells transfected with the NiV-N or N-S451A plasmid. The expression levels of each N protein and GAPDH are shown. Error bars indicate standard deviations. n.s., not significant. N-S451A-expressing Cos7 cells were treated with 2,000 U/ml of IFN-α. N-S451A and STAT1 were detected with specific antibodies and are shown as z-stack immunofluorescence images. Arrowheads and arrows indicate an N-S451A-expressing and a non-N-S451A-expressing cell, respectively. The experiment was independently conducted three times. (E) The expression plasmids for NiV-N and EGFP-Kir/Gem-W268G (referred to here as rKir/Gem) were transfected into Cos7 cells, and NiV-N was detected with an anti-NiV-N polyclonal antibody. The nuclei were stained with Hoechst dye. Images shown are z-stack data. The arrowheads and arrows point to a NiV-N-expressing and a non-NiV-N-expressing cell, respectively. The bar graph indicates the statistical evaluation of the rKir/Gem distribution. The scores were determined by counting approximately 60 cells from five randomly selected fields. n.s., not significant.

Article Snippet: The following antibodies were purchased: rabbit antibodies against STAT1 p84/p91 (E-23 [sc-346]; Santa Cruz), phospho-STAT1 (Tyr701) (9171; Cell Signaling Technology), STAT2 (C-20 [sc-476]; Santa Cruz), p-Stat2 (Tyr690) (sc-21689-R; Santa Cruz), STAT3 (H-190 [sc-7179]; Santa Cruz), histone H3 (D1H2) (4499P; Cell Signaling Technology), tubulin (H300 [sc-5546]; Santa Cruz), PKR (D-20 [sc-708]; Santa Cruz), HA tag (631207; Clontech), and c-Myc tag (C3956; Sigma-Aldrich); a rabbit IgG isotype control antibody (ab37415-5; Abcam); and mouse antibodies against STAT1α p91 (C-111 [sc-417]; Santa Cruz), STAT2 (A-7 [sc-1668] and A-9 [sc-166201]; Santa Cruz), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (MAB374; Millipore), HA tag (H9654; Sigma-Aldrich), and c-Myc (631206; Clontech).

Techniques: Immunoprecipitation, Construct, Negative Control, Positive Control, Transfection, Binding Assay, Reporter Assay, Plasmid Preparation, Expressing, Immunofluorescence, Staining

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