SAB2500450
Anti-GAPDH, C-Terminal antibody produced in goat
affinity isolated antibody, buffered aqueous solution
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Synonym(s):
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
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
goat
Quality Level
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)
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.
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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Regulatory Information
含少量动物源组分生物产品
常规特殊物品
Certificates of Analysis (COA)
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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)
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)
Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA Repair.
Kosova A A, et al.
Biochemistry. Biokhimiia, 82(6), 643-654 (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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