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G5262

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GAPDH

standard for protein electrophoresis

Synonym(e):

Glyceraldehyd-3-Phosphat-Dehydrogenase aus Kaninchenmuskel, GAP-DH

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32

Qualität

for molecular biology

Qualitätsniveau

Form

powder

Mol-Gew.

~36 kDa

Verpackung

vial of 5 mg

Methode(n)

electrophoresis: suitable

Lagertemp.

2-8°C

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Allgemeine Beschreibung

GAPDH (Glyceraldehyde-3-phosphate dehydrogenase) catalyzes the conversion of glyceraldehyde-3-phosphate into D-glycerate-1,3-bisphosphate as part of the glycolysis pathway. GAPDH has also been found to function in additional cellular process, such as transcription, apoptosis, oxidative stress and ER to Golgi transport.

Anwendung

GAPDH protein is suitable for use as a molecular weight marker and protein standard for molecular biology applications, including western blotting and mass spectometry.

Biochem./physiol. Wirkung

Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate into D-glycerate-1,3-bisphosphate as part of the glycolysis pathway.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Ling Ji et al.
Molecular therapy. Nucleic acids, 19, 546-561 (2020-01-14)
Long non-coding RNAs (lncRNAs) are crucial molecules in tumorigenesis and tumor growth in various human cancers, including colorectal cancer (CRC). Studies have revealed that lncRNAs can regulate cellular processes in cancers by interacting with proteins, for example RNA-binding proteins (RBPs).
Wen-Wei Zhang et al.
Eukaryotic cell, 12(1), 70-77 (2012-11-06)
The initial 7 steps of the glycolytic pathway from glucose to 3-phosphoglycerate are localized in the glycosomes in Leishmania, including step 6, catalyzed by the enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In L. donovani and L. mexicana, there exists a second GAPDH
Kati Juuti-Uusitalo et al.
Investigative ophthalmology & visual science, 54(5), 3510-3519 (2013-05-21)
Aquaporins (AQPs), a family of transmembrane water channel proteins, are essential for allowing passive water transport through retinal pigmented epithelial (RPE) cells. Even though human native RPE cells and immortalized human RPEs have been shown to express AQPs, the expression
S A Ismail et al.
Acta crystallographica. Section D, Biological crystallography, 61(Pt 11), 1508-1513 (2005-10-22)
The crystal structure of human liver glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been determined. This structure represents the first moderate-resolution (2.5 A) and crystallographically refined (Rfree = 22.9%) human GAPDH structure. The liver GAPDH structure consists of a homotetramer, each subunit of
J E Welch et al.
Journal of andrology, 21(2), 328-338 (2000-03-14)
Although the process of glycolysis is highly conserved in eukaryotes, several glycolytic enzymes have unique structural or functional features in spermatogenic cells. We previously identified and characterized the mouse complementary DNA (cDNA) and a gene for 1 of these enzymes

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