Aprotinin from bovine lung
SIGMA/A1153 - lyophilized powder, 3-8 TIU/mg solid
Synonym: BPTI; Bovine pancreatic trypsin inhibitor; Trasylol; Trypsin inhibitor (basic)
CAS Number: 9087-70-1
Empirical Formula (Hill Notation): C284H432N84O79S7
Molecular Weight: 6511.44
EC Number: 232-994-9
MDL Number: MFCD00130541
Linear Formula: C284H432N84O79S7
Product Type: Chemical
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. Aprotinin is a single peptide chain with three disulfide bonds. Molecular Weight: ~6511
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: A1153-100MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: A1153-250MG
| biological source | bovine lung |
| form | lyophilized powder |
| InChI key | ZPNFWUPYTFPOJU-UHFFFAOYSA |
| mol wt | ~6,500 |
| Quality Level | 300  |
| solubility | H2O: ≥5 mg/mL |
| specific activity | 3-8 TIU/mg solid |
| storage temp. | 2-8°C |
| UniProt accession no. | P00974  |
| 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 |
| Application: | 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. |
| 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. |
| 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. |
| Packaging: | 1, 5 mg in glass bottle |
| Packaging: | 10, 25, 100, 250 mg in poly bottle |
| 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. |
| 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-argini |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: 3-8 TIU/mg solid |
| Storage Temp. | 2-8°C |
| UNSPSC | 12352202 |