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C3777

Sigma-Aldrich

Casein fluorescein isothiocyanate from bovine milk

Type II, essentially salt-free, lyophilized powder

Synonym(s):

FITC-casein

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About This Item

MDL number:
MFCD00130743
UNSPSC Code:
12352204
NACRES:
NA.32

type

Type II

Quality Level

200

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Sigma-Aldrich

C6554

Casein from bovine milk

Thomas S Murray et al.
Journal of medical microbiology, 59(Pt 5), 511-520 (2010-01-23)
Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen capable of acutely infecting or persistently colonizing susceptible hosts. P. aeruginosa colonizes surfaces in vitro by either biofilm formation or swarming motility. The choice of behaviour is influenced by the physical properties of
Invited review: Understanding the behavior of caseins in milk concentrates
Corredig M, et al.
Journal of Dairy Science, 102(6), 4772-4782 (2019)
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
Hui Gao et al.
Plant physiology, 173(1), 219-239 (2016-11-23)
Aspartic proteases are a class of proteolytic enzymes with conserved aspartate residues, which are implicated in protein processing, maturation, and degradation. Compared with yeast and animals, plants possess a larger aspartic protease family. However, little is known about most of
Michael Maurer et al.
Cell chemical biology, 26(8), 1169-1179 (2019-06-18)
ATP-driven bacterial AAA+ proteases have been recognized as drug targets. They possess an AAA+ protein (e.g., ClpC), which threads substrate proteins into an associated peptidase (e.g., ClpP). ATPase activity and substrate selection of AAA+ proteins are regulated by adapter proteins

Protocols

Substrates Procedures

Our General Protease Assay Procedures and Substrates overview.

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