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82452

Proteinase K, immobilized on Eupergit® C from Tritirachium album

powder (granular), ≥1500 U/g

Sinonimo/i:

Endopeptidase K, immobilized on Eupergit® C

Autenticati per visualizzare i prezzi organizzativi e contrattuali.

Informazioni su questo articolo

NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥1500 U/g
Biological source:
fungus (Tritirachium album)


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.[1]

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


pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Classe di stoccaggio

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



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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)
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



Numero articolo commerciale globale

SKUGTIN
82452-1G04061822646346

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