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G5262

Supelco

GAPDH

standard for protein electrophoresis

Sinónimos:

Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle, D-Glyceraldehyde 3-phosphate:NAD+ oxidoreductase (phosphorylating), GAPDH

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About This Item

Número de CAS:
9001-50-7
Comisión internacional de enzimas:
1.2.1.12 (BRENDA, IUBMB)
EC Number:
232-609-4
MDL number:
MFCD00131203
UNSPSC Code:
12352204
NACRES:
NA.32

grade

for molecular biology

Quality Level

200

form

powder

mol wt

~36 kDa

packaging

vial of 5 mg

technique(s)

electrophoresis: suitable

storage temp.

2-8°C

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General description

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.

Application

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 Actions

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

related product

Referencia del producto
Descripción
Precios

P7170

Ponceau S solution, BioReagent, suitable (for use in cellulose acetate electrophoresis), 0.1 % (w/v) in 5% acetic acid

C8302

4-Chloro-1-naphthol solution, For HRP detection on Western Blots

P7059

Disolución salina tamponada con fosfato, 10× PBS for Western blots and IP

B5655

SIGMAFAST™ BCIP®/NBT, tablet

B6404

BCIP®/NBT solution, premixed

RPROB

Reversible Protein Detection Kit for Membranes and Polyacrylamide Gels

W0138

Western Blocker™ Solution, for HRP detection systems

SDS7B2

Prestained Molecular Weight Marker, mol wt 26,600-180,000 Da

C1992

Marcador de electroforesis ColorBurst™, mol wt 8,000-220,000 Da

GERPN2209

ECL™ Western Blotting Detection Reagents, Cytiva RPN2209

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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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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).
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
Craig Nicholls et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(33), 13308-13313 (2012-08-01)
Oxidative stress regulates telomere homeostasis and cellular aging by unclear mechanisms. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key mediator of many oxidative stress responses, involving GAPDH nuclear translocation and induction of cell death. We report here that GAPDH interacts with
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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