anti-Ferredoxin Reductase, mAb (6C2)

CHF 322.00
In stock
YIF-LF-MA0033100 µlCHF 322.00
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Product Details
Synonyms AR; ADXR; FDXR; EC=1.18.1.6; Ferredoxin Reductase; Adrenodoxin Reductase; Ferredoxin-NADP(+) Reductase; NADPH:adrenodoxin Oxidoreductase, Mitochondrial
Product Type Monoclonal Antibody
Properties
Clone 6C2
Isotype Mouse IgG1 κ
Immunogen/Antigen Recombinant human fragment protein purified from E. coli.
Application

ELISA
Western Blot (1:1,000)
IHC-P

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
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
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

Ferredoxin reductase is a ubiquitous flavoenzyme, containing noncovalently bound FAD as a prosthetic group (1). It plays a role in delivering NADPH or low potential one-electron donors such as ferredoxin and flavodoxin to redox-based metabolisms in plastids, mitochondria and bacteria (2). In mammals, ferredoxin reductase is loosely associated with the inner mitochondrial membrane and receives electrons from NADPH. These electrons are transferred to ferredoxin which shuttles electrons to cytochrome P450 in the adrenal cortex mitochondrial steroid hydroxylation systems (3). Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-β hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.

Product References

1) Carrillo, N. and Ceccarelli, E. D. (2003) Eur. J. Biochem. 270, 1900-1915. (General)
2) Lambeth, J. D. and Kamin, H. (1977) J.Biol. Chem. 252, 2908-2917. (General)
3) Lin, D. et al. (1990) Proc. Natl. Acad. Sci. USA. 87, 8516-8520. (General)

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