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82452

Sigma-Aldrich

Proteinase K, immobilized on Eupergit® C from Tritirachium album

powder (granular), ≥1500 U/g

Sinónimos:

Endopeptidase K, immobilized on Eupergit® C

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Tritirachium album)

form

powder (granular)

specific activity

≥1500 U/g

storage temp.

2-8°C

General description

Proteinase K is secreted extracellular medium by mold, Tritirachium album. It hydrolyses keratin and shows substrate specificity similar to serine alkaline proteinases.

Application

Proteinase K, immobilized on Eupergit® C from Tritirachium album has been used:
  • in the protolysis of human serum
  • in the digestion of gruel samples for enzyme linked immune assays (ELISA)
  • in proteolytic stability studies of calcium ion flux inducers

Biochem/physiol Actions

Proteinase K hydrolyses keratin by cleaving peptide bonds adjacent to the carboxyl group of aliphatic and aromatic amino acids.

Unit Definition

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol N-acetyl-L-tyrosine-ethylester (ATEE) per minute at pH 9.0 and 30 °C.

Legal Information

Eupergit is a registered trademark of Röhm GmbH & Co. KG

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Enterococcus faecium stimulates human neutrophils via the formyl-peptide receptor 2
Bloes DA, et al.
Testing, 7(6), e39910-e39910 (2012)
Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
MoriharaKand Tsuzuki, Hiroshige
Agricultural and Biological Chemistry, 39(7), 1489-1492 (1975)
Isolation and thermal stability studies of two novel serine proteinases from the fungus Tritirachium album Limber
Samal BB, et al.
Enzyme and Microbial Technology, 13(1), 66-70 (1991)
Lysophosphatidic acid cooperates with 1alpha, 25 (OH) 2D3 in stimulating human MG63 osteoblast maturation
Gidley J, et al.
Prostaglandins & other lipid mediators, 80(1-2), 46-61 (2006)
Neil T Sprenkle et al.
Journal of neurochemistry, 148(4), 516-530 (2018-12-07)
Improper protein folding and trafficking are common pathological events in neurodegenerative diseases that result in the toxic accumulation of misfolded proteins within the lumen of the endoplasmic reticulum (ER). While low-level stimulation of the unfolded protein response (UPR) is protective

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