Description
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. It is present in blood and in most tissues, with a high concentration in lung, inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins. Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512 Daltons. Aprotinin is purified by proprietary chromatographic techniques.
Biomolecule/Target: N/A
Synonyms: Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP
Alternates names: Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP
Taglines: An inhibitor of trypsin and related proteolytic enzymes
NCBI Gene ID #: N/A
NCBI Gene Symbol: N/A
Gene Source: N/A
Accession #: N/A
Recombinant: No
Source: Bovine lung
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: 98%
Assay #2: HPLC
Endotoxin Level: <0.1 ng/g
Activity (Specifications/test method): N/A
Biological activity: 5 x 10 IU/mg.
Results: 6 x 10 IU/mg.
Binding Capacity: N/A
Unit Definition: N/A
Molecular Weight: 6.5 kDa
Concentration: N/A
Appearance: Lyophilized protein
Physical form description: Sterile filtered and lyophilized with no additives
Reconstitution Instructions: Reconstitute in HO to a concentration of 1 mg/ml. The solution can then be diluted into other aqueous buffers and store at 4°C for 1 week or 20°C for future use. For long-term storage, it is recommend to add a carrier protein (e.g., 0.1% BSA). Prevent freeze/thaw cycles.
Amino acid sequence: N/A