82452
Proteinase K, immobilized on Eupergit® C from Tritirachium album
powder (granular), ≥1500 U/g
别名:
Endopeptidase K, immobilized on Eupergit® C
产品名称
Proteinase K, immobilized on Eupergit® C from Tritirachium album, powder (granular), ≥1500 U/g
biological source
fungus (Tritirachium album)
form
powder (granular)
specific activity
≥1500 U/g
storage temp.
2-8°C
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.
General description
Proteinase K is secreted extracellular medium by mold, Tritirachium album. It hydrolyses keratin and shows substrate specificity similar to serine alkaline proteinases.
Other Notes
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
法规信息
新产品
此项目有
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)
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
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.
Prostaglandins & other lipid mediators, 80(1-2), 46-61 (2006)
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