Aprotinin from bovine lung
SIGMA/SRE0050 - saline solution, 3-7 TIU/mg protein
Synonym: Aprotinin from bovine lung; BPTI; Bovine pancreatic trypsin inhibitor; Trasylol; Trypsin inhibitor (basic)
CAS Number: 9087-70-1
Empirical Formula (Hill Notation): C284H432N84O79S7
Molecular Weight: 6511.44
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
Elevate Quality Program Icon
| assay | 1-3 mg/mL protein (biuret) |
| biological source | bovine (calf) lung |
| bovine lung | |
| color | almost colorless |
| description | For research or further manufacturing use only. Not intended for direct use in humans or animals. Non-TSCA use only in US. |
| form | saline solution |
| InChI key | ZPNFWUPYTFPOJU-UHFFFAOYSA |
| mol wt | ~6,500 |
| Quality Level | 400  |
| shipped in | wet ice |
| SMILES string | S1SCC2NC(=O)CNC(=O)CNC(=O |
| solubility | water: soluble at 20 °C |
| specific activity | 3-7 TIU/mg protein |
| storage condition | dry at room temperature |
| protect from light at room temperature | |
| storage temp. | 2-8°C |
| Application: | Aprotinin is largely used as an inhibitor of trypsin. |
| 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, also known as pancreatic trypsin inhibitor and trypsin-kallikrein inhibitor, is a monomeric polypeptide of 58 amino acids found in a number of organs, including lungs, spleen, liver, and pancreas. It is also detectable in a free form in calf serum. It is a competitive inhibitor that forms a loose complex with serine proteases and blocks their active centers. The complex exhibits many interactions between protease and inhibitor. The trypsin-aprotinin complex, for example, does not dissociate at a concentration of 8 M uric acid or 6 M guanidine hydrochloride. Aprotinin is only cleaved slowly by most proteases, with the exception of thermolysin at temperatures >+60°C. Its unique structure is responsible for the molecule’s high stability and remarkable resistance to elevated temperatures, acids, and proteases. |
| Other Notes: | 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 | nwg |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | 1-3 mg/mL protein (biuret) |
| activity | specific activity: 3-7 TIU/mg protein |
| Storage Temp. | 2-8°C |
| UNSPSC | 12352200 |