欧美自拍另类欧美宗合图片区,国产视频一区二区三区四区,日本一区二区三区四区视频,婬片一区AAA毛片一区二区

商品編號


YIF-LF-P0008



品牌


Adipogen



公司


Adipogen



公司分類(lèi)


Proteins



Size

0.5 mg

商品信息


More Information



Product Details



Synonyms

GAPD; GAPDH; EC=2.6.99.-; EC=1.2.1.12; Peptidyl-Cysteine S-Nitrosylase GAPDH; Glyceraldehyde-3-Phosphate Dehydrogenase



Product Type

Protein



Properties



Source/Host

E. coli



Crossreactivity

Human



BIOLOG
ical Activity

43.96U/mg (One unit of activity of GAPDHis defined as the amount of enzyme required to convert 1 μmole of NAD to NADH per minunder standard assay conditions)



Formulation

Lyophilized in 20mM HEPES, pH 7.4.



Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.



Declaration

Manufactured by AbFrontier



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

-20°C



Handling Advice

Avoid freeze/thaw cycles.



Use/St
ABI
lity

After reconstitution, store at -80°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37-kDa subunits. GAPDH catalyzes the revers
IBL
e reduction of 1,3-bisphosphoglycerate to glyceraldehydes 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, this ubiquitously expressed enzyme also displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication, DNA repair, nuclear RNA export, membrane fusion and microtubule bundling (1-5). Other studies also provide evidence of GAPDH playing an essential part of the program of gene expression observed in apoptosis and as part of the cellular phenotype of age-related neuro-degenerative diseases (6-7).


Product References
1) Baxi, M. D. and Vishwanatha, J. K. (1995) Biochemistry. 34, 9700-9707. (General)
2) McNulty, S. E. and Toscano, W. A. Jr. (1995) Biochem. Biophys. Res. Commun. 34, 165-171. (General)
3) Singh, R. and Green, M. R. (1993) Science. 259, 365-368. (General)
4) Zang, W. Q. et al. (1998) Virology. 28, 46-52. (General)
5) Han, X. et al. (1998) Biochem. Biophys. Acta. 1414, 95-107. (General)
6) Kragten, E. et al. (1998) J. Biol. Chem. 273, 5821-5828. (General)
7) Koshy, B. (1996) Hum. Mol. Genet. 5, 1311-1318. (General)
8) Bagui, S. et al. (1999) Eur. J. Biochem. 262(2), 386-395. (General)