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SRE0024

Glyceraldehyde-3-phosphate dehydrogenase human

recombinant, expressed in Escherichia coli

Synonym(s):

D-Glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), GAPDH, Triosephosphate dehydrogenase

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100 μG

$539.00

$539.00


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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
1.2.1.12
Specific activity:
≥80 units/mg protein
Recombinant:
expressed in E. coli

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recombinant

expressed in E. coli

specific activity

≥80 units/mg protein

storage temp.

−20°C

Quality Level

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This Item
G6019G5262G2267
specific activity

≥80 units/mg protein

specific activity

50-150 units/mg protein

specific activity

-

specific activity

≥75 units/mg protein

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) localizes to the cytoplasm but can be translocated to the nucleus depending on cellular conditions. It is a tetramer containing identical chains. The gene encoding GAPDH is localized on human chromosome 12p13.[1]

Application

Human glyceraldehyde-3-phosphate dehydrogenase has been used as a positive control for hydrogen sulfide treatment to detect sulfhydration of protein targets.[2]

Biochem/physiol Actions

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the reversible oxidative phosphorylation of glyceraldehyde-phosphate, which is a critical energy-yielding step in carbohydrate metabolism. It binds to several proteins including actin, tubulin, amyloid precursor, polyglutamine peptides, DRPLA (dentatorubral-pallidoluysian atrophy) and huntingtin.[3] Phosphorylated GAPDH associates with cytoskeletal elements and controls microtubule dynamics in the early secretory pathway.[4] GAPDH is also a component of the functional GAIT (interferon-?-activated inhibitor of translation) mRNP (messenger ribonucleoprotein).[5] GAPDH expression is dysregulated during melanoma progression.[6]

Physical form

This product is recombinant, human GAPDH expressed in E. coli with an N-terminal histidine tag and has a predicted molecular mass of 37,984 Da. The product is lyophilized from a buffered solution with stabilizers.

Other Notes

Alternative number: CAS Number 9001-50-7
One unit will reduce 1.0 μmole of 3-phosphoglycerate to D-glyceraldehyde 3-phosphate per minute in a coupled system with 3-phosphoglyceric phosphokinase (3-PGK) at pH 7.6 at 25 °C

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Eye Irrit. 2

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Gennaro Napolitano et al.
EMBO molecular medicine, 7(2), 158-174 (2015-01-15)
Metabolite accumulation in lysosomal storage disorders (LSDs) results in impaired cell function and multi-systemic disease. Although substrate reduction and lysosomal overload-decreasing therapies can ameliorate disease progression, the significance of lysosomal overload-independent mechanisms in the development of cellular dysfunction is unknown
Joana Alves et al.
PloS one, 10(12), e0144196-e0144196 (2015-12-18)
Group B Streptococcus (GBS), a commensal organism, can turn into a life-threatening pathogen in neonates and elderly, or in adults with severe underlying diseases such as diabetes. We developed a vaccine targeting the GBS glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme
Nuclear-translocated glyceraldehyde-3-phosphate dehydrogenase promotes poly (ADP-ribose) polymerase-1 activation during oxidative/nitrosative stress in stroke.
Nakajima H, et al.
The Journal of Biological Chemistry, 290(23), 14493-14503 (2015)
Mutant huntingtin: nuclear translocation and cytotoxicity mediated by GAPDH.
Bae B, et al.
Proceedings of the National Academy of Sciences of the USA, 103(9), 3405-3409 (2006)
Hydrogen sulfide inhibits Kir2 and Kir3 channels by decreasing sensitivity to the phospholipid PIP2.
Ha J, et al.
The Journal of Biological Chemistry, RA117-RA117 (2018)

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