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A1153

Sigma-Aldrich

Aprotinin

3-8 TIU/mg solid, lyophilized powder

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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:
UNSPSC Code:
12352202
NACRES:
NA.77

product name

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

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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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

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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RNAPro? SAL: A device for rapid and standardized collection of saliva RNA and proteins
Chiang SH, et al.
Biotechniques, 58(2), 69-76 (2015)
Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
Agic D, et al.
Journal of Biomolecular Structure & Dynamics, 8(1), 1-11 (2019)
Engineering of a biomimetic pericyte-covered 3D microvascular network
Kim J,
PLoS ONE, 10(7), e0133880-e0133880 (2015)
The effects of cell death-inducing DNA fragmentation factor-alpha-like effector C (CIDEC) on milk lipid synthesis in mammary glands of dairy cows
Yang Y, et al.
Journal of Dairy Science, 100(5), 4014-4024 (2017)
Perioperative systemic haemostatic agents
Mahdy AM and Webster NR
British journal of anaesthesia, 93(6), 842-858 (2004)

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.

Elastase application index for understanding leukocyte elastase, a 29KDa serine endoprotease.

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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