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Key Documents

SAB4300645

Sigma-Aldrich

Anti-GAPDH antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-G3PD, Anti-GAPD, Anti-MGC88685

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~37 kDa

species reactivity

human, rat, mouse

concentration

1 mg/mL

technique(s)

western blot: 1:500-1:1000

isotype

IgG

immunogen sequence

(P-A-K-Y-D)

NCBI accession no.

UniProt accession no.

shipped in

wet 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 , that is located on chromosome 12p13. It is basically called as a glycolytic enzyme.

The antibody detects endogenous level of total GAPDH protein.

Immunogen

Peptide sequence around aa. 252-256 (P-A-K-Y-D), according to the protein NP_002037.2

Application

Anti-GAPDH antibody has been used in western blotting.{60,61}

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.

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.

Target description

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC By similarity. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate.

Physical form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The S113R mutation (c.339T>G) (MIM #603690.0001) in SLC33A1 (MIM #603690), an ER membrane acetyl-CoA transporter, has been previously identified in individuals with hereditary spastic paraplegia type 42 (SPG42; MIM #612539). SLC33A1 has also been shown to inhibit the bone morphogenetic
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Icariin, a flavonoid isolated from the traditional Chinese herbal medicine Epimedium brevicornum Maxim, has been shown to possess anti-inflammatory, anti‑oxidant and anti-atherosclerotic activities in vivo and in vitro. The aim of the present study was to investigate the effects of
Role of Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) in DNA Repair
Kosova AA, et al.
Biochemistry. Biokhimiia (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 (2017)
Increased copy number of the TERT and TERC telomerase subunit genes in cancer cells
Cao Y, et al.
Cancer Science (2008)

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