Skip to Content
Merck
CN

11610

Azo-Casein

protease substrate

Synonym(s):

Azocasein

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.26
MDL number:
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


biological source

bovine

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


Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

常规特殊物品

This item has



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

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