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C3777

Sigma-Aldrich

Casein fluorescein isothiocyanate from bovine milk

Type II, essentially salt-free, lyophilized powder

Synonyme(s) :

FITC-casein

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About This Item

Numéro MDL:
MFCD00130743
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Type

Type II

Forme

essentially salt-free, lyophilized powder

Ampleur du marquage

20-50 μg FITC per mg solid

Solubilité

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

Température de stockage

2-8°C

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Description générale

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

Actions biochimiques/physiologiques

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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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

Protocoles

Substrates Procedures

Our General Protease Assay Procedures and Substrates overview.

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