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A1153

Sigma-Aldrich

Aprotinin from bovine lung

lyophilized powder, 3-8 TIU/mg solid

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Synonym(s):
BPTI, Bovine pancreatic trypsin inhibitor, Trasylol, Trypsin inhibitor (basic)
Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
EC Number:
MDL number:
NACRES:
NA.77

biological source

bovine lung

Quality Level

form

lyophilized powder

specific activity

3-8 TIU/mg solid

mol wt

~6,500

solubility

H2O: ≥5 mg/mL

UniProt accession no.

storage temp.

2-8°C

InChI key

ZPNFWUPYTFPOJU-UHFFFAOYSA-N

Gene Information

cow ... PTI(404172)

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1 of 4

This Item
A6279A4529SRE0078
Aprotinin from bovine lung lyophilized powder, 3-8 TIU/mg solid

A1153

Aprotinin from bovine lung

Aprotinin from bovine lung saline solution, 3-7 TIU/mg protein

A6279

Aprotinin from bovine lung

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

A4529

Aprotinin from bovine lung

Aprotinin from bovine lung lyophilized powder, ≥3 TIU/mg solid, Suitable for manufacturing of diagnostic kits and reagents

SRE0078

Aprotinin from bovine lung

Gene Information

cow ... PTI(404172)

Gene Information

cow ... PTI(404172)

Gene Information

cow ... PTI(404172)

Gene Information

-

Quality Level

300

Quality Level

300

Quality Level

-

Quality Level

400

form

lyophilized powder

form

saline solution

form

lyophilized powder

form

lyophilized powder

solubility

H2O: ≥5 mg/mL

solubility

H2O: soluble >10 mg/mL

solubility

H2O: >10 mg/mL

solubility

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

General description

Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa. Commonly used as a non-specific serine protease inhibitor, aprotinin contains an antiparallel β sheet, N-terminal 310 helix and C-terminal and α helix. Aprotinin residues from amino acids 13 - 18 are essential for binding to serine proteases.

Application

Aprotinin from bovine lung has been used:
  • as a protease inhibitor in radioimmunoprecipitation assay buffer (RIPA) for the homogenization of cardiac microvascular endothelial cells (CMECs)(4) and mammary epithelial cells
  • in angiogenesis assay for fibroblast
  • in the proteomic stabilization of saliva supernatant

Aprotinin is largely used as an inhibitor of trypsin.

Biochem/physiol Actions

Aprotinin inhibits proteases like trypsin, plasmin, chymotrypsin and thrombin. It blocks the bradykinin synthesis from kininogen. It is useful for treating blood loss during surgery.
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 a lyophilized powder with activity of 3-8 TIU/mg of solid powder. Aprotinin is freely soluble in water (>10 mg/mL) and in aqueous buffers of low ionic strengths. Dilute solutions tend to be less stable than concentrated ones, though solution stability also depends on pH. Aprotinin is relatively stable against denaturation - only thermolysin has been found capable of degrading it at 60-80°C. Sterilizaiton of Aprotinin can be achieved through filtration by a 0.2 μm filter.

also commonly purchased with this product

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

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Articles

While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung.

Enzyme Explorer Product Application Index for Elastase. Leukocyte elastase is a 29KDa serine endoprotease of the Proteinase S1 Family. It exists as a single 238 amino acid-peptide chain with four disulfide bonds.

ReadyShield® phosphatase and protease inhibitor cocktail FAQ for sample protection in a variety of cell types and tissue extracts, including mammalian, plant, and microbial samples. Our ReadyShield® Protease Inhibitor Cocktail is a non-freezing solution that contains inhibitors with a broad specificity for serine, cysteine, acid proteases and aminopeptidases.

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Protocols

Objective: To standardize a procedure for the enzymatic assay of Aprotinin.

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