Anti gapdh ab

Manufactured by Thermo Fisher Scientific

Anti-GAPDH Ab is a primary antibody that specifically binds to the GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) protein. GAPDH is a commonly used housekeeping gene and its expression is often used as a loading control in various molecular biology techniques.

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Lab products found in correlation

Anti ha, by Merck Group (3 mentions) Anti ha, by Roche (3 mentions) Anti α2δ 1 ab, by Merck Group (3 mentions) α2δ 1 ab, by Merck Group (2 mentions) Alexa fluor 594 anti rabbit, by Thermo Fisher Scientific (2 mentions) Alexa fluor 488 anti rat, by Thermo Fisher Scientific (2 mentions) Anti mouse alexa fluor 647, by Thermo Fisher Scientific (2 mentions) Anti flag ab, by Merck Group (2 mentions) Anti g97, by Abcam (2 mentions) Bml ei300, by Enzo Life Sciences (2 mentions) Bmei325, by Enzo Life Sciences (2 mentions) Bml ei302, by Enzo Life Sciences (2 mentions) Alexa fluor 594 anti rat, by Thermo Fisher Scientific (2 mentions) Anti pdi, by Thermo Fisher Scientific (2 mentions) ω conotoxin gvia, by Alomone (1 mentions) Anti pdi, by Abcam (1 mentions) Anti akt ab, by Cell Signaling Technology (1 mentions) Anti mouse alexa fluor 488, by Thermo Fisher Scientific (1 mentions) Anti ha ab, by Roche (1 mentions) Typhoon 9410 phosphorimager, by GE Healthcare (1 mentions)

Spelling variants of this product

GAPDH (1486 citations) Anti-GAPDH (220 citations)

5 protocols using anti gapdh ab

Immunodetection of Ca2+ Channel Subunits

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Ca channel Abs used were: α₂δ-1 Ab (mouse monoclonal against α₂-1 moiety, Sigma-Aldrich, epitope identified in (Cassidy et al., 2014 (link))), anti-Ca_V2.2 II-III loop Ab (rabbit polyclonal) (Raghib et al., 2001 (link)). A bespoke, affinity-purified Cachd1 rabbit polyclonal Ab was raised by Cambridge Research Biochemicals (Billingham, UK) against the predicted extracellular domain of zCachd1 protein, produced by transient transfection of mammalian cells (Durocher et al., 2002 (link)) (G.T.P., S.W.W., and Gavin J. Wright, unpublished data). Purified Ab activity was confirmed by enzyme-linked immunosorbent assay. Other Abs used were anti-HA (rat monoclonal, Roche), anti-HA (rabbit polyclonal, Sigma), anti-GAPDH Ab (mouse monoclonal, Ambion), and GFP Ab (Living Colors, rabbit polyclonal; BD Biosciences). For immunocytochemistry, secondary Abs (1:500) used were anti-rabbit-Alexa Fluor 594, anti-rat-Alexa Fluor 488, anti-mouse-Alexa Fluor 647 (Life Technologies) or anti-rat fluorescein isothiocyanate (Sigma-Aldrich). The secondary Abs used for Western Blotting were goat anti-rabbit, goat anti-rat, and goat-anti-mouse Abs coupled to horseradish peroxidase (HRP) (Biorad). ω-conotoxin GVIA was purchased from Alomone, and applied by local perfusion.

Dahimene S., Page K.M., Kadurin I., Ferron L., Ho D.Y., Powell G.T., Pratt W.S., Wilson S.W, & Dolphin A.C. (2018). The α2δ-like Protein Cachd1 Increases N-type Calcium Currents and Cell Surface Expression and Competes with α2δ-1. Cell Reports, 25(6), 1610-1621.e5.

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Immunodetection of Ca2+ Channel Subunits

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Antibodies (Abs) used were: anti-Ca_V2.2 II-III loop Ab (rabbit polyclonal) (Raghib et al., 2001 (link)), anti-Ca_V2.1 II-III loop Ab (rabbit polyclonal, Alomone), anti- α₂δ-1 Ab (mouse monoclonal, Sigma-Aldrich), anti-HA (rat monoclonal, Roche), anti-HA (rabbit polyclonal, Sigma), anti-PDI (mouse monoclonal, Abcam), anti-Akt Ab (rabbit polyclonal, Cell Signaling Technology) and anti-GAPDH Ab (mouse monoclonal, Ambion). For immunocytochemistry, secondary Abs (1:500) used were anti-rabbit-Alexa Fluor 594, anti-rat- Alexa Fluor 488, anti-rat-Alexa Fluor 594 and 647 and anti-mouse-Alexa Fluor 488 (ThermoFisher). For immunoblotting, secondary Abs (1:2000) were anti-rabbit-Horseradish Peroxidase (HRP), and anti-mouse HRP (Biorad).

Meyer J.O., Dahimene S., Page K.M., Ferron L., Kadurin I., Ellaway J.I., Zhao P., Patel T., Rothwell S.W., Lin P., Pratt W.S, & Dolphin A.C. (2019). Disruption of the Key Ca2+ Binding Site in the Selectivity Filter of Neuronal Voltage-Gated Calcium Channels Inhibits Channel Trafficking. Cell Reports, 29(1), 22-33.e5.

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Antibody-Based Detection of Adhesion Proteins

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Antibodies (Abs) used were: Anti-α₂δ-1 Ab (mouse monoclonal, Sigma-Aldrich), anti-α₂δ-3 and anti-δ-3 Ab,^{8 (link)} anti-HA Ab (rat monoclonal, Roche), anti-GAPDH Ab (mouse monoclonal, Ambion), anti-FLAG Ab (rabbit polyclonal; Sigma), anti-PDI (mouse monoclonal, Ambion), anti-g97 (rabbit polyclonal; Abcam), and anti-flotillin Ab (monoclonal, BD Biosciences). For immunoblotting, secondary Abs (1:2000) were anti-rabbit–Horseradish Peroxidase (HRP), and anti-mouse HRP (Biorad). For immunocytochemistry, anti-rat-Alexa Fluor 594 was used at 1/500 (ThermoFisher).
The metalloprotease inhibitors GM6001 (BML-EI300, Enzo Life Sciences), SB-3CT (BMEI325, Enzo Life Sciences), and MMP-13 inhibitor (BML-EI302, Enzo Life Sciences) were dissolved in DMSO (or water for MMP-13 inhibitor) and used at the concentrations stated. N-TIMP-3 protein (expressed in Escherichia coli as previously described,^{38 (link)}) or control samples in the absence of N-TIMP-3, were preincubated with heparin (200 µg/ml) for an hour at 37°C before adding to the cells.

Kadurin I., Dahimene S., Page K.M., Ellaway J.I., Chaggar K., Troeberg L., Nagase H, & Dolphin A.C. (2022). ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary α2δ Subunits, and Enables Calcium Current Enhancement. Function, 3(3), zqac013.

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Antibody Characterization for Calcium Channels

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Ca channel antibodies (Abs) used were: α₂δ-1 Ab (mouse monoclonal against α₂-1 moeity, Sigma-Aldrich, epitope identified in [Cassidy et al., 2014 (link)]), α₂-3 (71–90) Ab (rabbit; polyclonal) (Davies et al., 2010 (link)), δ-3 (1035–1049) Ab (Davies et al., 2010 (link)), anti-Ca_V2.2 II-III loop Ab (rabbit polyclonal) (Raghib et al., 2001 (link)). Other Abs used were anti-HA (rat monoclonal, Roche), anti-HA (rabbit polyclonal, Sigma), anti-GAPDH Ab (mouse monoclonal, Ambion), anti-flotillin-1 (mouse monoclonal, BD Biosciences), and GFP Ab (Living Colors, rabbit polyclonal; BD Biosciences). For immunocytochemistry, secondary Abs (1:500) used were anti-rabbit-Alexa Fluor 594, anti-rat-Alexa Fluor 594, anti-mouse-Alexa Fluor 647 (Life Technologies) or fluorescein isothiocyanate (FITC)-anti-rat (Sigma-Aldrich). The following secondary Abs were used for western blot: goat anti-rabbit, goat anti-rat and goat anti-mouse Abs coupled to horseradish peroxidase (HRP) (Biorad, Hemel Hempstead, UK). The signal was obtained by HRP reaction with fluorescent product (ECL 2; Thermo Scientific) and membranes were scanned on a Typhoon 9410 phosphorimager (GE Healthcare). Lyophilized active thrombin was obtained from Sigma, suspended in filter-sterilised PBS (Sigma; pH7.4) to 1000 U/ml and frozen in aliquots until use.

Kadurin I., Ferron L., Rothwell S.W., Meyer J.O., Douglas L.R., Bauer C.S., Lana B., Margas W., Alexopoulos O., Nieto-Rostro M., Pratt W.S, & Dolphin A.C. (2016). Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels. eLife, 5, e21143.

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Investigating Metalloprotease Inhibitors on Cell Signaling

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Antibodies (Abs) used were: anti-α2δ-1 Ab (mouse monoclonal, Sigma-Aldrich), anti-α2δ-3 and anti-δ-3 Ab (Davies et al., 2010) , Ab anti-HA Ab (rat monoclonal, Roche), anti-GAPDH Ab (mouse monoclonal, Ambion), anti-FLAG Ab (rabbit polyclonal; Sigma), anti-PDI (mouse monoclonal, Ambion), anti-g97 (rabbit polyclonal; Abcam), anti-flotillin Ab monoclonal, BD Biosciences). For immunoblotting, secondary Abs (1:2000) were anti-rabbit-Horseradish Peroxidase (HRP), and antimouse HRP (Biorad). For immunocytochemistry, anti-rat-Alexa Fluor 594 was used at 1/500 (ThermoFisher).
The metalloprotease inhibitors GM6001 (BML-EI300, Enzo Life Sciences), SB-3CT (BMEI325, Enzo Life Sciences) and MMP-13 inhibitor (BML-EI302, Enzo Life Sciences) were dissolved in DMSO (or water for MMP-13 inhibitor) and used at the concentrations stated. N-TIMP-3 protein (expressed in E. coli as previously described (Kashiwagi et al., 2001) , or control samples in the absence of N-TIMP-3, were pre-incubated with heparin (200 µg/ml) for an hour at 37 o C before adding to the cells.

Kadurin I., Dahimène S., Page K.M., Ellaway J.I.J., Chaggar K., Troeberg L., Nagase H., & Dolphin A. (2021). Identification that ADAM17 mediates proteolytic maturation of calcium channel auxiliary α₂δ subunits, and enables calcium current enhancement.

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