Recombinant Human Biliverdin reductase A(BLVRA) CSB-EP002721HU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Biliverdin-IX alpha-reductase
Species: (Organism)
Homo sapiens (Human)
Gene Names:
BLVRA
Tag info:
N-terminal GST-tagged
Target Protein AA Sequence:
MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
Expression Region:
1-296aa
Subcellular Location:
Cytoplasm
Tissue Specificity:
Liver.
Protein Length:
Full Length
Pathway:
Mol. Weight:
60.4 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Signal Transduction
Function:
Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
Involvement in disease:
Hyperbiliverdinemia (HBLVD)
Relevance:
Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Gfo/Idh/MocA family, Biliverdin reductase subfamily
Reference:
"Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes." Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr. Eur. J. Biochem. 235:372-381(1996)
