NAD Kinase (catalytic domain) (human) (rec.) (His) (highly active)
| Code | Size | Price |
|---|
| AG-40T-0090-C050 | 50 ug | £390.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Regulatory Status: RUO
Target Species: Human
Shipping:
Blue Ice
Storage:
-20°C
Documents
Further Information
Alternate Names/Synonyms:
NADK; Poly(P)/ATP NAD Kinase; EC 2.7.1.23
Biological Activity:
>2U/mg protein. One unit is defined as the amount of enzyme that synthesizes 1µmol of NADP per min.
Concentration:
1mg/ml
EClass:
32160000
Endotoxin:
N/A. Free of any nucleotide converting side-activities.
Form (Short):
liquid
Formulation:
Liquid. Ammonium sulphate suspension.
Handling Advice:
After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.
Long Description:
Protein. Human NAD kinase (aa 64-446) is fused at the N-terminus to a His-tag. Source: E. coli. Endotoxin content: N/A. Free of any nucleotide converting side-activities. Liquid. Ammonium sulphate suspension. Purity: >95% (SDS-PAGE). NAD kinase catalyzes the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis.
Molecular Weight:
~42kDa (monomer)
NCBI, Uniprot Number:
O95544
Package Type:
Plastic Vial
Product Description:
NAD kinase catalyzes the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis.
Purity:
>95% (SDS-PAGE)
Sequence:
Human NAD kinase (aa 64-446) is fused at the N-terminus to a His-tag.
Source / Host:
E. coli
TAGs:
His
Transportation:
Non-hazardous
UNSPSC Category:
Other Enzymes
UNSPSC Number:
12352204
Use & Stability:
Working aliquots are stable for up to 3 months when stored at -20°C.
References
Structural and functional characterization of human NAD kinase: F. Lerner, et al.; BBRC 288, 69 (2001) | NADPH regulates human NAD kinase, a NADP+-biosynthetic enzyme: K. Ohashi, et al.; Mol. Cell Biochem. 355, 57 (2011)