Enzymes. This group offers enzymes, used in all types of PCRs, and/or used in different isolation stages, like lysozyme and RNase A enzyme.

Showing all 8 results

DNJia FFPE Tissue Kit

HunteRNase-P, Recombinant

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.

DNJia FFPE Tissue Kit

HunteRNase, Recombinant

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.

DNJia FFPE Tissue Kit

Hy-Fidelity Pfu Polymerase, Recombinant

 16,900,000 67,620,000

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.

DNJia FFPE Tissue Kit

Hy-Taq Polymerase, Recombinant

 2,430,000 4,370,000

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.

DNJia FFPE Tissue Kit

Lysozyme, lyophilized powder

 6,573,600

ROJE lysozyme possesses the ability of breaking down bacteria cell wall through hydrolyzing peptidoglycans. This product also hydrolyses chitodextrin.

DNJia FFPE Tissue Kit

Proteinase K, Recombinant

 3,258,000

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.

DNJia FFPE Tissue Kit

RJ-Protease, Recombinant

 3,908,400

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.