Enzymes. This group offers enzymes, used in all types of PCRs, and/or used in different isolation stages, like lysozyme and RNase A enzyme.
HunteRNase-P is an enhanced recombinant RNase inhibitor developed from Human placenta. This ROJE product inhibits the activity of RNases A, B and C. This Inhibitor cannot inhibit RNases T1, T2, U1, U2, CL3 and prokaryotic RNases I and H.
HunteRNase inhibits the activity of RNases A, B and C at 1:1 ratio. This recombinant protein cannot inhibit RNases T1, T2, U1, U2, CL3 and prokaryotic RNases I and H.
Hy-Fidelity Pfu Polymerase is an engineered version of pfu DNA polymerase with enhanced yield and higher fidelity. It possesses a proofreading 3’-5’ exonuclease activity.
Recombinant Hy-Taq polymerase is purified from E. coli expressing cloned DNA polymerase from Thermus aquaticus. The enzyme consists of a single polypeptide with molecular weight of approximately 94kDa. It has 5’-3’ DNA polymerase activity and 5’-3’ exonuclease activity. It lacks 3’-5’ exonuclease activity. This enzyme is suitable for routine amplification.
ROJE lysozyme possesses the ability of breaking down bacteria cell wall through hydrolyzing peptidoglycans. This product also hydrolyses chitodextrin.
Prime-RNase A (20mg/ml) is an endonuclease degrading single strand RNA in biological samples to prevent RNA contamination. This product has shown no DNase activity.
This Product exhibits broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups.
RJ-Protease an engineered version of Proteinase k exhibiting as broad substrate specificity as wild type proteinase k. It show higher stability than proteinase k in the presence of detergents. The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups.