Proteinase K, >30 mAnson U/mg

Proteinase K, >30 mAnson U/mg

Synonyms Endopeptidase K; Proteinase, Tritirachium album serine

CAS Number: 39450-01-6 Molecular Weight: ~30 kDa

EC Number: 254-457-8 MDL Number: 8.9

SKU 02193504-CF
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Description

Product Description

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.

Application Notes

Proteinase K is suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Addition of either 0.5-1% of sodium dodecyl sulfate or 1-4 mmol/l of urea increases the activity, because the substrates are more easily attacked when denatured. In experiment to recover the undigested DNA, proteins were digested with 0.1 mg/ml of proteinase K.

Usage Statement

Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.

Key Applications

Protein and nucleic acid isolation

Specifications
SKU 02193504-CF
Alternate Names Endopeptidase K; Proteinase, Tritirachium album serine
Application Notes Proteinase K is suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Addition of either 0.5-1% of sodium dodecyl sulfate or 1-4 mmol/l of urea increases the activity, because the substrates are more easily attacked when denatured. In experiment to recover the undigested DNA, proteins were digested with 0.1 mg/ml of proteinase K.
Base Catalog Number 193504
Biochemical Physiological Actions Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.
CAS # 39450-01-6
EC Number 254-457-8
Format <5 × 10-4 u/mg
Gel Strength <5 × 10-4 u/mg
Insoluble Matter H315-H319-H334-H335
Molecular Weight ~30 kDa
Optical Rotation 219398190
pKa Dust mask type , Eyeshields, Faceshields, Gloves
Potency pH optimum (denatured hemoglobin as substrate): pH 7.5-12.00
Source Danger
Specific Activity Soluble in water (1 mg/mL)
Specificity Proteinase K cleaves peptide bonds mostly after the carboxyl group of N-substituted hydrophobic aliphatic and aromatic amino acids; as shown by specificity trials with amino acid-4-nitroacilides. Thus; it shows similarities with alkaline Asperigillus proteases. However; unlike the latter; Protease K also cleaves peptide amides; comparable to the alkaline serine-proteases from Bacillus species. The specificity of ester cleavage is also high.
Sterility Tritirachium album
Sterilization of Solutions >30 mAnson u/mg
Usage Statement Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.