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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:
9087-70-1
Molecular Weight:
6511.44
EC Number:
232-994-9
MDL number:
MFCD00130541
NACRES:
NA.77

biological source

bovine lung

Quality Level

300

form

lyophilized powder

specific activity

3-8 TIU/mg solid

mol wt

~6,500

solubility

H2O: ≥5 mg/mL

UniProt accession no.

P00974

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

Product No.
Description
Pricing

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)

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  1. When using Product A1153, Aprotinin from bovine lung, what is the conversion from KIU to TIU? 

    According to data from our labs here at Sigma, there are approximately 1300 KIU per 1 TIU.  This, along with other useful information, can be found on the product information sheet available at our website:  A1153 Product Information Sheet  

  2. Is Aprotinin from bovine lung, Product A1153, the same as Trasylol?

    Trasylol is the Bayer AG registered trademark name for this material.

  3. How should I store solutions of Aprotinin from bovine lung, Product A1153?

    Sterile solutions of aprotinin may be stored at 4 °C or as frozen aliquots at -20 °C.

  4. What are typical concentrations of Aprotinin from bovine lung, Product A1153, to use as a protease inhibitor?

    Typical concentration of Aprotinin to be used as a protease inhibitor is 1 μM or approximately 6.5 μg/ml.

  5. What type of inhibitor is Aprotinin from bovine lung, Product A1153?

    Aprotinin is a competitive serine protease inhibitor which forms stable complexes that block the active site of the enzyme. 

  6. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  7. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  8. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  9. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  10. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

J Pyo et al.
Journal of dairy science, 103(5), 4236-4251 (2020-03-17)
This study evaluated how feeding colostrum- or a colostrum-milk mixture for 3 d postnatal affects plasma glucagon-like peptide-2 (GLP-2), serum insulin-like growth factor-1 (IGF-1), and small intestinal histomorphology in calves. Holstein bulls (n = 24) were fed colostrum at 2
Perioperative systemic haemostatic agents
Mahdy AM and Webster NR
British journal of anaesthesia, 93(6), 842-858 (2004)
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)
M Rafiq Islam et al.
Scientific reports, 9(1), 11596-11596 (2019-08-14)
Protease inhibitors, such as trypsin inhibitor, serum alpha-1 antitrypsin, or liver aprotinin, are a class of proteins that competitively bind and block the catalytic activity of proteolytic enzymes with wide ranging biological functions. A significant number of protease inhibitors have
View All Related Papers

Articles

Aprotinin

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

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

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.

Chymotrypsin

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

Protocols

Enzymatic Assay of Aprotinin

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

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