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SAB2500450

Sigma-Aldrich

Anti-GAPDH, C-Terminal antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Sinónimos:

G3PD, GAPD, Glyceraldehyde-3-phosphate dehydrogenase, HEL-S-162eP, HGNC:4141, MGC88685, aging-associated gene 9 protein, epididymis secretory sperm binding protein Li 162eP, peptidyl-cysteine S-nitrosylase GAPDH

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

goat

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, rat

species reactivity (predicted by homology)

canine, pig

technique(s)

immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GAPDH(2597)

Categorías relacionadas

General description

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional protein and is encoded by the gene mapped to human chromosome 12p13. It is basically called as a glycolytic enzyme.

Immunogen

Peptide with sequence C-HQVVSSDFNSDT from the C Terminus of the protein sequence according to NP_002037.2.

application

Recommended concentration:
Western Blot 0.01-0.5ug/uL
Immunohistochemistry 5 ug/mL
Immunofluorescence 5 ug/mL
Optimal dilutions/concentrations should be determined by the end user.
Anti-GAPDH, C-Terminal antibody produced in goat has been used in single cell western blot analysis.

Biochem/physiol Actions

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in DNA repair. It is essential for the sixth step of glycolysis. It participates in transcriptional and posttranscriptional gene regulation. It also controls intracellular membrane trafficking and cell death. Accumulation of GAPDH results in mitochondrial dysfunction. Phosphorylated GAPDH associates with cytoskeletal elements and controls microtubule dynamics in the early secretory pathway. GAPDH is also a component of the functional GAIT (interferon-γ-activated inhibitor of translation) mRNP (messenger ribonucleoprotein). GAPDH expression is dysregulated during melanoma progression.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Chi-Chih Kang et al.
NPJ precision oncology, 2, 10-10 (2018-06-07)
In addition to canonical oncoproteins, truncated isoforms and proteolysis products are implicated in both drug resistance and disease progression. In HER2-positive breast tumors, expression of truncated HER2 isoforms resulting from alternative translation and/or carboxy-terminal fragments (CTFs) resulting from proteolysis (collectively
High-selectivity cytology via lab-on-a-disc western blotting of individual cells.
Kim J J, et al.
Lab on a chip, 17(5), 855-863 (2017)
Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA Repair.
Kosova A A, et al.
Biochemistry. Biokhimiia, 82(6), 643-654 (2017)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) aggregation causes mitochondrial dysfunction during oxidative stress-induced cell death.
Nakajima H, et al.
The Journal of Biological Chemistry, 292(11), 4727-4742 (2017)
Increased copy number of the TERT and TERC telomerase subunit genes in cancer cells.
Cao Y, et al.
Cancer Science, 99(6), 1092-1099 (2008)

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