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Bovine Aprotinin (from Lung), MP Biomedicals
Bovine Aprotinin (from Lung), MP Biomedicals
Catalog # IC0219455910
Supplier:  MP Biomedicals
CAS Number:  
Bovine Aprotinin (from Lung), MP Biomedicals
Catalog # IC0219455910
Supplier:  MP Biomedicals
Supplier Number:  0219455910
CAS Number:  

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Specifications

  • Pack type:
    Bottle
  • Source:
    Lung
  • Species:
    Bovine
  • Size:
    10 mg
  • Biological Activity:
    ~4 inhibitor U/mg
  • Protein/Peptide Name:
    Aprotinin
  • Grade:
    Cell Culture Reagent
  • Cat. No.:
    IC0219455910
  • Supplier no.:
    0219455910

Specifications

About this item

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes with, and blocks the active sites of serine protease enzymes. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage.

  • White Powder
  • EINECS: 232-994-9
  • pH: 5.0 - 7.0 (1% aq soln)
  • Isoelectric Point: 10.5(Lit.)
  • Storage temperature: +4 °C
  • UV/Visible Absorbance, λ max (water): 277 ± 5 nm
  • Extinction Coefficient, E1% (280 nm): 8.3 (water)(Lit.)
  • Soluble in water (10 mg/mL - completely soluble) and in aqueous buffers of low ionic strengths
  • Typical Working Concentration: Effective Concentration is Equimolar with protease (1-2 µg/mL)
  • Sterilization of Solutions: Sterilization of solutions can be done by filtration through a 0.2 µm filter
  • Kallikrein Inactivating Unit (KIU): One KIU is identical to the quantity of protease inhibitor that has the ability to inhibit 2 Kallikrein units by 50% under optimal conditions

Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin

It is used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.

Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3.