Protease from Streptomyces griseus 

Literature see 81748, Pronase

Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.

• highly stable in pH range of 5.0 to 9.0, with peak activity at pH 8.8
• compatible with many DNA and RNA isolation buffers
• broad substrate specificity

Collected from culture broth of S. griseus and purified by successive column procedures.

A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.

1 U corresponds to the amount of enzyme which liberates 1 μmol folin-positive amino acids and peptides (calculated as tyrosine) per minute at pH 7.5 and 37°C (casein, Fluka No. 22078, as substrate)

Completely inactivated by heating above 80 °C for 15-20 minutes.

BioChemika

powder

M_r 15000-27000

~25% Calcium acetate

light brown

−20°C

2

UK9595000