ADH1C Human, sf9

ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
Catalog Number: AS-P00097
Lead time: 3-4 business days
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$0.00
ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Products specifications
Expression host Sf9, Baculovirus cells.
Purity Greater than 95.0% as determined by analysis by SDS-PAGE.
Formulation ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Synonyms ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Reagent Appearance Sterile Filtered clear solution.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino acid sequence MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR TVLTFHHHHH H.
Assay Solution's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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