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United States 

Bestatin . hydrochloride

Aminopeptidase inhibitor
 
ALX-260-012-M005 5 mg 107.00 USD
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Replaces Prod. #: BML-EI212

Inhibits aminopeptidases like aminopeptidase B, leucine aminopeptidase, tripeptide aminopeptidase, aminopeptidases on the surface of mammalian cells. Does not inhibit carboxypeptidases. May be used in in vitro translation system to inhibit the aminopeptidases found in reticulocate or wheat germ lysates. Activates macrophages and T lymphocytes. Immunomodulator. Has antitumor properties and enhances not only blastogenesis and lymphocytes in vitro, but also establishes a delayed-type hypersensitivity in vivo.

Product Details

Alternative Name:[(2S,3R)-3-Amino-2-hydroxy-4-phenylbutanoyl]-L-leucine . HCl
 
Formula:C16H24N2O4. HCl
 
MW:308.4 . 36.5
 
Source:Synthetic.
 
CAS:65391-42-6
 
Purity:≥98% (HPLC)
 
Appearance:White to off-white powder.
 
Solubility:Soluble in methanol, acetic acid, DMSO, dimethyl formamide or 100% ethanol; slightly soluble in water.
 
Shipping:Ambient Temperature
 
Long Term Storage:-20°C
 
Use/Stability:Stock solutions in organic solvents are stable for 1 month at -20°C. We do not recommend storing aqueous solutions for more than one day.
 
Handling:Protect from light.
 
Regulatory Status:RUO - Research Use Only
 
ALX-260-012
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ALX-260-012

Product Literature References

3-Amino-2-hydroxy-propionaldehyde and 3-amino-1-hydroxy-propan-2-one derivatives: new classes of aminopeptidase inhibitors: C. Tarnus, et al.; Bioorg. Med. Chem. 4, 1287 (1996), Abstract;
Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes: L. Orning, et al.; J. Biol. Chem. 266, 1375 (1991), Abstract;
The slow, tight binding of bestatin and amastatin to aminopeptidases: S.H. Wilkes & J.M. Prescott; J. Biol. Chem. 260, 13154 (1985), Abstract;
Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes: D.H. Rich, et al.; J. Med. Chem. 27, 417 (1984), Abstract;
Low-molecular-weight enzyme inhibitors of microbial origin: H. Umezawa; Ann. Rev. Microbiol. 36, 75 (1982), Abstract;
Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes: H. Umezawa, et al.; J. Antibiot. 29, 97 (1976), Abstract;

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