C3777
Casein fluorescein isothiocyanate from bovine milk
Type II, essentially salt-free, lyophilized powder
Synonym(s):
FITC-casein
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
Quality Level
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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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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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)
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
Swarming motility, secretion of type 3 effectors and biofilm formation phenotypes exhibited within a large cohort of Pseudomonas aeruginosa clinical isolates
Murray T S, et al.
Journal of Medical Microbiology, 59(Pt 5), 511-511 (2010)
Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal
Vega LA and Caparon MG
Molecular Microbiology, 85(6), 1119-1132 (2012)
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