Guinea pig L-Asparaginase
Recombinant full length (aa 1-565) guinea pig L-asparginase purified by nickel-sepharose chromatography.
Highlights:
- Highly pure - >99% (SDS-PAGE)
- High L-asparaginase activity with low KM (~50 µM) for Asn
- Very low L-glutaminase activity
Asparaginase (EC 3.5.1.1, 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.
Recombinant full length (aa 1-565) guinea pig L-asparginase purified by nickel-sepharose chromatography.
Highlights:
- Highly pure - >99% (SDS-PAGE)
- High L-asparaginase activity with low KM (~50 µM) for Asn
- Very low L-glutaminase activity
Asparaginase (EC 3.5.1.1, 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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Specifications
| Product Type: | Protein |
| Name: | Guinea pig L-asparaginase |
| Accession ID: | H0W0T5 |
| Source: | Recombinant expression in E. coli |
| Molecular Weight: | ~63 kDa |
| Amino Acid Sequence: | MARASGSERHLLLIYTGGTLGMQSKGGVLVPGPGLVTLLRTLPMFHDKEFAQAQGLPDHALALPPASHGPRVLYTVLECQPLLDSSDMTIDDWIRIAKIIERHYEQYQGFVVIHGTDTMASGASMLSFMLENLHKPVILTGAQVPIRVLWNDARENLLGALLVAGQYIIPEVCLFMNSQLFRGNRVTKVDSQKFEAFCSPNLSPLATVGADVTIAWDLVRKVKWKDPLVVHSNMEHDVALLRLYPGIPASLVRAF |
| Fusion Tag(s): | N-terminal His tag |
| Purity: | >99% (SDS-PAGE) |
| Buffer: | 25 mM Tris pH7.5, 500 mM NaCl, 2 mM DTT, 1 mM EDTA |
| Concentration: | 4.4mg/mL |
| 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. |
| Storage: | -80C |
| Shipped: | Dry ice |
Data
SDS-PAGE Analysis
Provider
From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago.
References
- Schalk AM, Nguyen HA, Rigouin C, Lavie A. Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties. J Biol Chem. 2014 Nov 28;289(48):33175-86. doi: 10.1074/jbc.M114.609552. Epub 2014 Oct 15.
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