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Merck

C3777

Sigma-Aldrich

Casein fluorescein isothiocyanate from bovine milk

Type II, essentially salt-free, lyophilized powder

Sinónimos:

FITC-casein

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About This Item

MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

type

Type II

form

essentially salt-free, lyophilized powder

extent of labeling

20-50 μg FITC per mg solid

solubility

water: 5 mg/mL, clear to hazy, yellow to orange

storage temp.

2-8°C

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General description

Casein is a major milk phospho-protein and constitutes about 80% of the total protein content in milk. Bovine milk is composed of four types of casein such as, αS1, αS2, β, and κ. Casein exists as micelles in milk.

Application

Casein fluorescein isothiocyanate from bovine milk has been used:
  • as a substrate for semi-quantitative analysis of protease in Arabidopsis cells
  • to determine the caseinolytic activity of secreted LasB (elastase), alkaline protease and protease IV
  • for determining the SpeB (cysteine protease) proteolytic activity in Streptococcus pyogenes cells

highly sensitive protease substrate

Biochem/physiol Actions

Casein micelle system is involved in the prevention of pathological calcification of mammary glands.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

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Mark F Mabanglo et al.
Communications biology, 2, 410-410 (2019-11-23)
Bacterial ClpP is a highly conserved, cylindrical, self-compartmentalizing serine protease required for maintaining cellular proteostasis. Small molecule acyldepsipeptides (ADEPs) and activators of self-compartmentalized proteases 1 (ACP1s) cause dysregulation and activation of ClpP, leading to bacterial cell death, highlighting their potential
Laura Reinhardt et al.
mBio, 13(6), e0141322-e0141322 (2022-10-27)
Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp protease machinery has remained unsolved.
Invited review: Understanding the behavior of caseins in milk concentrates
Corredig M, et al.
Journal of Dairy Science, 102(6), 4772-4782 (2019)
Casein and Whey Proteins in Human Health
Milk and Dairy Products as Functional Foods, 102(6), 94-146 (2014)
Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal
Vega LA and Caparon MG
Molecular Microbiology, 85(6), 1119-1132 (2012)

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