BP000633-ENZ-252: Recombinant Human P4HB
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 512 amino acids (18-508 a.a.) and having a molecular mass of 57.5 kDa.
Purity > 90%, by SDS-PAGE.BP000632-ENZ-488: Recombinant Human ASPH
Source: E. coli-derived.
Purity > 90%, by SDS-PAGE.BP000620-ENZ-556: Recombinant Human Mitochondrial Short chain ECH 1
Source: E.coli-derived.
Purity > 95%, by SDS-PAGE.BP000606-ENZ-516: Recombinant Human FKBP6
Source: E. coli-derived.
Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.
Purity > 95%, by SDS-PAGE.BP000596-ENZ-483: Recombinant Human Phosphodiesterase 6D cGMP-Specific Rod Delta
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 158 amino acids (1-150 a.a.) and having a molecular mass of 18.4 kDa.
Purity > 90%, by SDS-PAGE.BP000580-ENZ-247: Recombinant Human MDH2
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 335 amino acids (25-338 a.a.) and having a molecular mass of 35.2 kDa.
Specific activity is > 30 units/mg, and is defined as the amount of enzyme that cleaves 1 umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH7.5 at 25C.
Purity > 95%, by SDS-PAGE.BP000561-ENZ-090: Recombinant Human Branched Chain keto Acid Dehydrogenase E1 Alpha
Source: E. coli-derived.
Purity > 80%, by SDS-PAGE.BP000556-ENZ-250: Recombinant Human Acyl-CoA Dehydrogenase Long Chain
Source: E. coli-derived.
Purity > 90%, by SDS-PAGE.BP000550-ENZ-413: Recombinant Human Dopa Decarboxylase
Source: E. coli-derived.
Purity > 95%, by SDS-PAGE.P000533-CKI-272B: Recombinant Human CKMT3
Source: Pichia Pastoris-derived.
The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000 ng/ml.
Purity > 95%, by RP-HPLC and SDS-PAGE.