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Proteinase K, Molecular biology reagent, >30 mAnson U/mg

Proteinase K, Molecular biology reagent, >30 mAnson U/mg

Synonyms Endoproteinase K

CAS Number: 39450-01-6 Molecular Weight: 626.511 g/mol

EC Number: 254-457-8 MDL Number: pI 8.9 (Lit.)

SKU 02193981-CF
$43.90
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Description

Product Description

Proteinase K

Application Notes

Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. It is also useful in removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A. It is reported to be useful for the isolation of hepatic, yeast, and mung bean mitochondria. It is useful in determination of enzyme localization on membranes. It is also used in treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. Proteinase K is used in digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

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

Isolation of DNA and RNA

Specifications
SKU 02193981-CF
Alternate Names Endoproteinase K
Application Notes Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. It is also useful in removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A. It is reported to be useful for the isolation of hepatic, yeast, and mung bean mitochondria. It is useful in determination of enzyme localization on membranes. It is also used in treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. Proteinase K is used in digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.
Base Catalog Number 193981
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
Extinction Coefficient E1%= 14.2 (280 nm,10 mM NaCl and 5 mM CaCl2, pH 8.0) (Lit.)
Format <5x 10-4 u/mgDNase
Gel Strength <5x10-4 u/mg
Gel Temperature Powder
Grade Molecular Biology Grade
Insoluble Matter H315-H319-H334-H335
Molecular Weight 626.511 g/mol
Optical Rotation 2193504
Particle Size Inhibition - Proteinase K belongs to the group of serine proteases with an easily esterifed serine fragment at the active center and, as with other proteases in this group, e.g. trypsin, chymotrypsin, is inactivated by diisopropylfluorophosphate or phenylmethane sulfonyl fluoride. Also inhibited by AEBSF and trypsin inhibitor. Metallic ion complexing agents, e.g., chelate formers such as EDTA and sulfhydryl reagents, have no effect on the activity of Proteinase K.
pKa Dust mask, Eyeshields, Faceshields, Gloves
Potency 7.5 -12.00 (denatured hemoglobin as substrate) (Lit.)
Source Danger
Specific Activity Soluble in water.
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.