Cofactors

Native, human iC3b complement component. iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein.

CRF, bovine (TFA) is a potent agonist of CRF receptor , and displaces [ 125 I-Tyr]ovine CRF with a K i of 3.52 nM.Appearance:SolidIC50&amp: Target:Ki: 3.52 nM (CRF receptor) .In Vitro:CRF, bovine is a potent agonist of CRF receptor, and displaces [

CRF, bovine (TFA) is a potent agonist of CRF receptor , and displaces [ 125 I-Tyr]ovine CRF with a K i of 3.52 nM.Appearance:SolidIC50&amp: Target:Ki: 3.52 nM (CRF receptor) .In Vitro:CRF, bovine is a potent agonist of CRF receptor, and displaces [

Ethyl 2-(4-bromo-2-formyl-6-methoxyphenoxy)acetate.

General DescriptionComplement factor H (fH) is purified from normal human serum. It is an essential regulatory component of the alternative pathway of complement. It is critical for prevention of complement activation on host cells and tissues,

Purity&gt:95% by SDS-PAGEExtinction Coeff. A280 nm = 1.43 at 1.0 mg/mL PrecautionsUse normal precautions for handling human blood productsGeneral DescriptionHuman factor I is purified from normal human serum (Fearon, D.T. (1977)). Factor I is a

Solubility in water: 5 g/lFlavin adenine dinucleotide (FAD) is used as a redox cofactor (electron carrier) by flavoproteins including succinate dehydrogenase (complex), α-ketoglutarate dehydrogenase, apoptosis-inducing factor 2 (AIF-M2, AMID),

Solubility in water: 5 g/lFlavin adenine dinucleotide (FAD) is used as a redox cofactor (electron carrier) by flavoproteins including succinate dehydrogenase (complex), α-ketoglutarate dehydrogenase, apoptosis-inducing factor 2 (AIF-M2, AMID),

Flavin adenine dinucleotide&nbsp(FAD) is a redox cofactor of flavoproteins, such as cytochrome-b 5 &nbspreductase enzyme. With the help of nicotinamide adenine dinucleotide phosphate (NADPH), FAD can be reduced to form FADH 2 .

Furfuryl Propionate.

Furfuryl Propionate.

Glucose-6-phosphate dehydrogenase (G6P DH) has an active dimeric form, whereas its monomeric and tetrameric forms are inactive. At low NADP + and NADPH levels and under normal conditions, the enzyme exists as equilibrium of tetramers and dimers,