ChemicalBook CAS DataBase List 39450-01-6

39450-01-6

Name	Proteinase K
CAS	39450-01-6
EINECS(EC#)	254-457-8
Molecular Formula	n.a.
MDL Number	MFCD00132129
Molecular Weight	626.505
MOL File	39450-01-6.mol

Chemical Properties

Appearance	Powder beige
storage temp.	2-8°C
solubility	H₂O: 10 mg/mL, slightly hazy, brown-yellow
form	powder
color	white
PH	pH7.5～12
Water Solubility	Miscible with water.
InChIKey	CDWGKFQEIBBJOF-BIZWTRPUNA-N
SMILES	N12[C@](OP(O)(OC3=CC=C([N+]([O-])=O)C=C3)=O)([C@H]([C@H](O)C)C1=O)[C@](C)(OC1=CC=CC=C1)C(OC1=CC=CC=C1)=C2C(OC)=O \|&1:1,16,17,22,r\|
CAS DataBase Reference	39450-01-6

Safety Data

Hazard Codes	Xn
Risk Statements	36/37/38-42 less more
Safety Statements	23-24-26-36/37-22-45 less more
WGK Germany	1
F	10
HS Code	35079090

Hazard Information

Chemical Properties

Powder beige

Description

Proteinase K is a proteolytic enzyme (a serine protease) naturally found in the mold Tritirachium album. In solution, it is stable over a pH range of 4.0–12.5 with an optimum of pH 8.0, and a temperature range of 25°C–65°C. The enzyme has two binding sites for Ca++, though in the absence of this divalent cation some catalytic activity is retained. Maximum proteinase K activity is observed with the inclusion of 1 mM Ca++ in the reaction buffer. Proteinase K digestion is routinely performed at 50°C, and occasionally in the presence of EDTA to inhibit labile, Mg++-dependent nucleases. Proteinase K is prepared commonly as a 20 mg/mL stock solution in sterile water (stable for 1 year at ?20°C) or in a solution of 50 mM Tris, pH 8.0, 1 mM CaCl2 (stable for months at 4°C). It is generally used at a working concentration of up to 50 μg/mL in any of a number of buffer formulations, including those that contain as much as 0.5% SDS[1].

Uses

A stable and highly reactive serine protease; used for protein and nucleic acid isolation.Proteinase K is used in the purification of RNA and DNA from tissues or cell lines. It finds application in protein modification, determination of enzyme localization and inactivation of RNases/DNases during nucleic acid extraction. It is also used in mitochondria isolation and removal of endotoxins bound to cationic proteins like lysozyme and ribonuclease A. Further, it is involved in the treatment of paraffin embedded tissue sections in order to expose antigen binding sites for antibody labeling.

Definition

Proteinase K cleaves peptide bonds next to the carboxyl-terminal of aromatic amino acids, hydrophobic amino acids and sulfuric amino acids, within the polypeptide chain. Hence Proteinase K can act as an endoprotease on a wide range of protein substrates. Because of its proteolytic preferences, it is a member of the subtilisin group of serine proteases. The K in Proteinase K refers to its ability to digest Keratin protein found in hairs, nails and hooves. Proteinase K is an essential reagent in molecular biology labs because it is useful in isolating DNA and RNA molecules by degrading and inactivating proteins. Fungus Tritirachium album Limber naturally produces proteinase K.

General Description

Proteinase K, an extracellular endopeptidase is synthesized by the mold, Tritirachium album Limber. Proteinase K belongs to a new subfamily of the subtilisins. It is a 277 amino acid protein and is characterized with an unhydrolyzed protein chain and autolyzed polypeptide chains.

Biochem/physiol Actions

Proteinase K catalyzes the hydrolysis of keratin.

References

[1] Farrell, R. “Creating a Ribonuclease-Free Environment.”RNA Methodologies (Sixth Edition) 2023: 51-70.

Material Safety Data Sheet(MSDS)

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