Recombinant full length (aa 1-565) guinea pig L-asparginase purified by nickel-sepharose chromatography.
Asparaginase (EC 18.104.22.168, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine (Asn) to aspartic acid. Asparagine has been shown to be essential for protein synthesis by some tumur cells which are unable to synthesize asparagine.
From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago.
Part of The Investigator's Annexe program.
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|Name:||Guinea pig L-asparaginase|
|Source:||Recombinant expression in E. coli|
|Molecular Weight:||~63 kDa|
|Amino Acid Sequence:||MARASGSERHLLLIYTGGTLGMQSKGGVLVPGPGLVTLLRTLPMFHDKEFAQAQGLPDHALALPPASHGPRVLYTVLECQPLLDSSDMTIDDWIRIAKIIERHYEQYQGFVVIHGTDTMASGASMLSFMLENLHKPVILTGAQVPIRVLWNDARENLLGALLVAGQYIIPEVCLFMNSQLFRGNRVTKVDSQKFEAFCSPNLSPLATVGADVTIAWDLVRKVKWKDPLVVHSNMEHDVALLRLYPGIPASLVRAF|
|Fusion Tag(s):||N-terminal His tag|
|Buffer:||25 mM Tris pH7.5, 500 mM NaCl, 2 mM DTT, 1 mM EDTA|
|Activity:||1,400 IU/mg protein; kcat= 24.5/sec with Asn as substrate; One unit of guinea pig L-asparaginase converts 1.0 µmole of Asn to Asp per minute at pH 7.5 at 37°C, as measured by a coupled enzyme system with 2 mM Asn as substrate.|
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