Skip to Content
Merck
CN
All Photos(1)

Documents

Safety Information

11610

Sigma-Aldrich

Azo-Casein

protease substrate

Synonym(s):

Azocasein

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.26

biological source

bovine

description

protease substrate

technique(s)

electrophoresis: suitable

solubility

water: 5 mg/mL

ε (extinction coefficient)

32-38 at 440 nm in 0.1 M NaOH at 1% (1 cm)

storage temp.

2-8°C

General description

Chromogenic substrate for proteolytic activity; Digestion results in the formation of colored components, which are soluble in trichloroacetic acid and determined (after neutralization) in the range 366 to 450 nm.

Application

Suitable as substrate for proteolytic enzymes and useful for post-electrophoretic detection of proteases.

Biochem/physiol Actions

Can be used to induce secondary amyloidosis in mice, in studies of amyloid protein processing.

Other Notes

Sales restrictions may apply

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

D Vázquez Peyronel et al.
Electrophoresis, 16(10), 1894-1897 (1995-10-01)
Azocasein, diffused into gels after polyacrylamide gel electrophoresis, provides a useful substrate for simple and rapid protease detection. After electrophoresis, the gels are incubated in an azocasein solution, immersed in trichloroacetic acid and then treated with NaOH. Proteolytic zones appear
Pineapple cysteine endopeptidases.
A D Rowan et al.
Methods in enzymology, 244, 555-568 (1994-01-01)
Fanqi Wang et al.
Immunology, 159(1), 109-120 (2019-10-14)
Serpins are evolutionarily conserved serine protease inhibitors that are widely distributed in animals, plants and microbes. In this study, we reported the cloning and functional characterizations of two novel serpin genes, HlSerpin-a and HlSerpin-b, from the hard tick Haemaphysalis longicornis
Shih-Hua Lo et al.
Animal bioscience, 35(10), 1592-1605 (2022-04-26)
The objective of this study was to select an effective in vitro digestion-fermentation model to estimate the effect of decreasing dietary crude protein (CP) on odor emission during pig production and to suggest potential prediction markers through in vitro and

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service