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A4529

Sigma-Aldrich

Aprotinin

3-7 TIU/mg solid, lyophilized powder

Synonym(s):

BPTI, Bovine pancreatic trypsin inhibitor, Trasylol, Trypsin inhibitor (basic)

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About This Item

Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.54

product name

Aprotinin from bovine lung, lyophilized powder, 3-7 TIU/mg solid

biological source

bovine lung

form

lyophilized powder

specific activity

3-7 TIU/mg solid

mol wt

~6,500

solubility

H2O: >10 mg/mL

UniProt accession no.

storage temp.

2-8°C

InChI key

ZPNFWUPYTFPOJU-UHFFFAOYSA-N

Gene Information

cow ... PTI(404172)

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Application

Aprotinin is largely used as an inhibitor of trypsin.

Biochem/physiol Actions

Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.

Unit Definition

One Trypsin Inhibitor Unit (TIU) will decrease the activity of two trypsin units by 50%, where one trypsin unit will hydrolyze 1.0 μmole of N-alpha-benzoyl-DL-arginine p-nitroanilide per minute at pH 7.8 and 25°C. Another commonly used unit is the KIU, with 1 TIU = 1,300 KIU.

Preparation Note

This product is an affinity purified lyophilized powder purified to remove trace impurities. It has an activity of 3-7 TIU/mg.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

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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The study of peptides presented by MHC class I and class II molecules is limited by the need for relatively large cell numbers, especially when studying post-translationally modified or otherwise rare peptide species. To overcome this problem, we pose the

Protocols

Enzymatic Assay of Aprotinin

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