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P4850

Sigma-Aldrich

Proteinase K from Tritirachium album

buffered aqueous glycerol solution, for molecular biology, ≥800 units/mL

Sinônimo(s):
Endopeptidase K
Número CAS:
Número da licença da enzima:
Número MDL:
NACRES:
NA.54

Nível de qualidade

200

grau

for molecular biology

forma

buffered aqueous glycerol solution

peso molecular

28.93 kDa

concentração

≥10 mg/mL
≥800 units/mL

Impurezas

≤0.5 ppm DNA (PicoGreen® assay)

atividade externa

DNase, Nickase and RNase, none detected

temperatura de armazenamento

2-8°C

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Aplicação

Proteinase K from Tritirachium album has been used:
  • in bovine endometrial epithelial cells for herpes viral DNA extraction
  • for viral RNA extraction from nasal swabs
  • as a component of phase lock and direct PCR lysis buffer

The product has been used to study its pre-treatment effects on the silk fibroin. The aspects analysed in this study included the crystallographic properties of hydroxyapatite (HAp), and the microstructure and microhardness of the composites. The enzyme has also been used to facilitate the access of probes to rRNA using FISH techniques to detect pathogenic Staphylococcus aureus.
Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.
Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria
Determination of enzyme localization on membranes
Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.
Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

Ações bioquímicas/fisiológicas

Proteinase K has a broad specificity and degrades many proteins even in the native state. It mainly cleaves the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked α-amino groups. The molecular weight of proteinase K from amino acid sequence is found to be 28,930 Da and from SDS-PAGE, it is found to be 28,500 Da. The optimum pH is between 7.5-9.0 and its isoelectric point is 8.9. Ca2+ (1-5 mM) is required for its activation. Proteinase K is inhibited by DIFP (diisopropylfluorophosphate) or PMSF (phenylmethylsulfonyl fluoride).
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.

Definição da unidade

One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

forma física

Solution in 40% glycerol (v/v) containing 10 mM Tris-HCl, pH 7.5, with 1 mM calcium acetate.

Informações legais

PicoGreen is a registered trademark of Life Technologies

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK Alemanha

WGK 1

Ponto de fulgor (ºF)

Not applicable

Ponto de fulgor (ºC)

Not applicable

Equipamento de proteção individual

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

Certificado de análise

Certificado de origem

M H Marana et al.
Fish & shellfish immunology, 105, 16-23 (2020-07-04)
Enteric redmouth disease (ERM), caused by the Gram negative enterobacterium Yersinia ruckeri, affects farming of salmonids, but vaccination against ERM confers a certain degree of protection dependent on the administration route. Recent studies on oral vaccination of rainbow trout suggest...
Robust Generation of Knock-in Cell Lines Using CRISPR-Cas9 and rAAV-assisted Repair Template Delivery
Vandemoortele G, et al.
Bio-protocol, 7(7), 1-6 (2017)
A S Neimanis et al.
Transboundary and emerging diseases, 65(1), 213-220 (2017-04-14)
Incursion of rabbit haemorrhagic disease virus (RHDV) into Sweden was documented in 1990 and it is now considered endemic in wild rabbit (Oryctolagus cuniculus) populations. Rabbit haemorrhagic disease virus 2 (RHDV2), a new, related lagovirus was first detected in France...
Bovine herpes virus type 4 alters TNF-alpha and IL-8 profiles and impairs the survival of bovine endometrial epithelial cells
Chanrot M, et al.
Reproductive Biology, 17(3), 225-232 (2017)
The first reported Florida clade 1 virus in the Nordic countries, isolated from a Swedish outbreak of equine influenza in 2011
Back H, et al.
Veterinary Microbiology, 184, 1-6 (2016)

Artigos

Enzymatic Assay of Proteinase K with Hemoglobin Substrate

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Protocolos

Enzymatic Assay of Proteinase K (EC 3.4.21.64)

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

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