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G5537

Sigma-Aldrich

Glyceraldehyde-3-phosphate Dehydrogenase from baker′s yeast (S. cerevisiae)

lyophilized powder, 70-140 units/mg protein

Synonym(e):

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

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About This Item

CAS-Nummer:
9001-50-7
EC-Nummer:
1.2.1.12 (BRENDA, IUBMB)
EG-Nummer:
232-609-4
MDL-Nummer:
MFCD00131203
UNSPSC-Code:
12352204

Form

lyophilized powder

Qualitätsniveau

200

Spezifische Aktivität

70-140 units/mg protein

Zusammensetzung

Protein, 30-70% biuret

Fremdaktivität

3-Phosphoglyceric phosphokinase ≤0.05%

Lagertemp.

−20°C

Biochem./physiol. Wirkung

Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles<<<,New>>>.

Einheitendefinition

One unit will reduce 1.0 μmole of 3-phosphoglycerate to D-glyceraldehyde 3-phosphate per min in a coupled system with 3-phosphoglyceric phosphokinase at pH 7.6 at 25 °C.

Physikalische Form

Lyophilized, sulfate-free powder stabilized with trehalose, citrate, and DTT. Useful for systems requiring low sulfate.

Inhibitor

Produkt-Nr.
Beschreibung
Preisangaben

I2512

Natriumjodacetat, ≥98%

Analysenzertifikate (COA)

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glycolysis metabolite

Sigma-Aldrich

D5764

2,3-Diphospho-D-glyceric acid pentasodium salt

D-(&#8722;)-3-Phosphoglycerinsäure Dinatriumsalz &#8805;93% dry basis (enzymatic), powder

Sigma-Aldrich

P8877

D-(−)-3-Phosphoglycerinsäure Dinatriumsalz

Enolase from baker’s yeast (S.&#160;cerevisiae) lyophilized powder, &#8805;50&#160;units/mg protein

Sigma-Aldrich

E6126

Enolase from baker′s yeast (S. cerevisiae)

D-Glyceraldehyd-3-phosphat -Lösung 8-13&#160;mg/mL in H2O

Sigma-Aldrich

39705

D-Glyceraldehyd-3-phosphat -Lösung

Kreatinphosphokinase aus Kaninchenmuskel Type I, salt-free, lyophilized powder, &#8805;150&#160;units/mg protein

Sigma-Aldrich

C3755

Kreatinphosphokinase aus Kaninchenmuskel

Lei Tong et al.
The Journal of biological chemistry, 284(17), 11256-11266 (2009-03-03)
Although the classical redox functions of co-enzyme NAD(+) are firmly established in metabolism, there are numerous enzymes that catalyze cleavage of NAD(+) to yield free ADP-ribose (ADPr) or related metabolites, whose functions remain largely unknown. Here we show that the
A Tarze et al.
Oncogene, 26(18), 2606-2620 (2006-10-31)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a pleiotropic enzyme that is overexpressed in apoptosis and in several human chronic pathologies. Here, we report that the protein accumulates in mitochondria during apoptosis, and induces the pro-apoptotic mitochondrial membrane permeabilization, a decisive event of
Bing Fang et al.
Biochimie, 95(2), 251-257 (2012-09-27)
siRNA is promising in anti-tumor therapy. The main challenge is lack of tumor-specific intracellular delivery. In this study, a 6 amino acids peptide (A1) with high affinity for vascular endothelial growth factor receptor-1 (VEGFR1) was conjugated with a cell penetrating
Milan Jirků et al.
The Journal of eukaryotic microbiology, 59(6), 537-547 (2012-08-01)
Several new species of trypanosomatids (Euglenozoa, Kinetoplastea, Trypanosomatidae), isolated from the intestines of Neotropical insects (Heteroptera), were genotyped on the basis of spliced leader RNA, and also defined phylogenetically using gene sequences of small subunit ribosomal RNA and glycosomal glyceraldehyde
Pablo Moreno-Acosta et al.
Anticancer research, 32(10), 4319-4325 (2012-10-13)
The aim of this study was to evaluate the predictive utility of Insulin-like growth factor-1 receptor (IGF1R), IGF1, IGF2, Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and of hemoglobin levels for tumor response to exclusive radiotherapy, in patients with locally advanced Human papillomavirus
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