82452
Proteinase K, immobilized on Eupergit® C from Tritirachium album
powder (granular), ≥1500 U/g
Synonym(s):
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Certificates of Analysis (COA)
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Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
MoriharaKand Tsuzuki, Hiroshige
Agricultural and Biological Chemistry, 39(7), 1489-1492 (1975)
Enterococcus faecium stimulates human neutrophils via the formyl-peptide receptor 2
Bloes DA, et al.
Testing, 7(6), e39910-e39910 (2012)
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)
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
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)
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