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A1153

Sigma-Aldrich

Aprotinin

3-8 TIU/mg solid, lyophilized powder

Synonym(s):

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

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1 MG
$72.70
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$227.00
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$465.00
100 MG
$1,560.00
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$3,960.00

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1 MG
$72.70
5 MG
$189.00
10 MG
$227.00
25 MG
$465.00
100 MG
$1,560.00
250 MG
$3,960.00

About This Item

Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

$72.70


In StockDetails


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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

SMILES string

S1SCC2NC(=O)CNC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C5NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C9N(CCC9)C(=O)CNC(=O)C(NC(=O)C(NC(=O)C%11N(CCC%11)C(=O

InChI

1S/C284H432N84O79S7/c1-21-144(9)222-271(439)337-174(68-46-105-309-282(300)301)239(407)340-187(120-160-77-85-164(374)86-78-160)251(419)341-185(116-156-55-29-24-30-56-156)250(418)342-188(121-161-79-87-165(375)88-80-161)252(420)346-191(123-208(291)378)246(41

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.[1] 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.[2] Aprotinin residues from amino acids 13 - 18 are essential for binding to serine proteases.[3]

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[4]
  • in angiogenesis assay for fibroblast[5]
  • in the proteomic stabilization of saliva supernatant[6]

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.[1] It is useful for treating blood loss during surgery.[3]
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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Certificates of Analysis (COA)

Lot/Batch Number

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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
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)
RNAPro? SAL: A device for rapid and standardized collection of saliva RNA and proteins
Chiang SH, et al.
Biotechniques, 58(2), 69-76 (2015)
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)

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.

Questions

1–7 of 7 Questions  
  1. What is the exact TIU/mg for the product? The information gives a range (3-8TIU/mg) but I need the exact value in order to calculate what size I need to order based on my samples.

    1 answer
    1. The exact value will be listed on the lot specific Certificate of Analysis. A Certificate can be accessed in the DOCUMENTATION section under 'Certificate of Analysis'. Please see the link below to access a specific lot or sample Certificate:
      https://www.sigmaaldrich.com/product/sigma/a1153#product-documentation

      Helpful?

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

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

      Helpful?

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

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

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

    1 answer
    1. 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

      Helpful?

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

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

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

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

      Helpful?

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

    1 answer
    1. 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.

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