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A2382

Sigma-Aldrich

Azoalbumin

protease substrate

Synonym(s):

Sulfanilic acid-azoalbumin

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

biological source

bovine

Quality Level

form

powder

concentration

60-90% (Lowry)

technique(s)

tissue culture: suitable

solubility

0.01 M HCl: soluble 25 mg/mL

storage temp.

2-8°C

General description

Azoalbumin is a substrate for assaying proteolytic enzymes, majorly trypsin, pepsin and cysteine proteinase. The assay method offers precision and is easy to perform.

Application

Azoalbumin has been used:
  • as a substrate for enzymatic assay of hyphal extracts
  • for screening general protease activity in spent growth medium extract
  • for screening S. rolfsii proteases

Preparation Note

Prepared from Bovine albumin, Fraction V (A 4503)

Substrates

A soluble chromogenic substrate for proteolytic enzymes.

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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B Cook et al.
Journal of reproduction and fertility, 51(1), 65-71 (1977-09-01)
No unusual steroid-binding proteins that might react with the oocyte or its investments could be detected in follicular fluid. Corticosteroid-binding globulin occurred in follicular fluid from pigs, sheep and cows, and sex hormone-binding globulin occurred in follicular fluid from sheep
Optimisation of cellobiose dehydrogenase production by the fungus Sclerotium (Athelia) rolfsii
Ludwig R and Haltrich D
Applied Microbiology and Biotechnology, 61(1), 32-39 (2003)
Inhibition of digestive trypsin-like proteases from larvae of several lepidopteran species by the diagnostic cysteine protease inhibitor E-64
Novillo C, et al.
Journal of Clinical Pathology, 27(3), 247-254 (1997)
Hydrolytic enzymes of leaf-cutting ant fungi
Erthal Jr M, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 152(1), 54-59 (2009)
Feces derived allergens of Tyrophagus putrescentiae reared on dried dog food and evidence of the strong nutritional interaction between the mite and Bacillus cereus producing protease bacillolysins and exo-chitinases
Erban T, et al.
Frontiers in Physiology, 7(3), 53-53 (2016)

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