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
Recommended Products
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Isotope dilution ESI-LC-MS/MS for quantification of free and total Nvarepsilon-(1-Carboxymethyl)-l-Lysine and free Nvarepsilon-(1-Carboxyethyl)-l-Lysine: Comparison of total Nvarepsilon-(1-Carboxymethyl)-l-Lysine levels measured with new method to ELISA assay in gruel samples
Tareke E, et al.
Food Chemistry, 141(4), 4253-4259 (2013)
Lysophosphatidic acid cooperates with 1alpha, 25 (OH) 2D3 in stimulating human MG63 osteoblast maturation
Gidley J, et al.
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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)
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)
Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
MoriharaKand Tsuzuki, Hiroshige
Agricultural and Biological Chemistry, 39(7), 1489-1492 (1975)
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