The product contains an asparaginase specific enzyme derived from Erwinia chrysanthemi. Specifically, this L-asparaginase is a tetrameric enzyme consisting of four identical subunits, each having a molecular weight of about 35 kDa.
<0.001 EU per 1 μg of the protein by the LAL method
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 2-8 °C for 1 week. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Asparaginase Erwinia chrysanthemi
The product is for the treatment of patients with acute lymphoblastic leukemia (ALL) that have developed a hypersensitivity to E. coli-derivied asparaginase. It is a component of a multi-agent chemotherpeutic regimen for the treatment of the aforementioned disease and is considered second- or third- line treatment in European and American protocols.
Examples of Clinical Use:
Acute lymphoblastic leukemia (ALL)
Asparagine is ordinarily found incorporated into most endogenous proteins. In its absence however, protein synthesis is halted - which in turn also results in the inhibition of the RNA and DNA synthesis necessary for cellular proliferation. One commonality between Acute Lymphoblastic Leukaemia (ALL), Acute Myeloid Leukaemia (AML), and Non-Hodgkin's Lymphoma (especially the lymphoblastic form) is the absence of asparagine synthetase activity in the neoplastic cells associated with these conditions. These neoplastic cells are subsequently dependent upon exogenous asparagine for their proliferation. The anti-neoplastic function of L-asparaginase is consequently a result of the sustained depletion of exogenous asparagine. In particular, Erwinia L-asparaginase catalyses the deamination of asparagine to aspartic acid and the release of an ammonia molecule. In addition, asparaginase also demonstrates a significant glutaminase activity in which it is capable of catalyzing the deamination of glutamine to glutamate and the release of an ammonia molecule. Since glutamine may lead to alternative asparagine synthesis, the ability for asparaginase to facilitate glutamine depletion may complement asparagine depletion. The exact potential to such glutaminase activity, however, remains unknown.
Mechanism of action:
Asparaginase Erwinia chrysanthemi catalyzes the deamidation of asparagine to aspartic acid and ammonia, resulting in a reduction in circulating levels of exogenous asparagine in the plasma. The mechanism of action of Erwinia asparaginase is thought to be based on the inability of leukemic cells to synthesize asparagine due to lack of asparagine synthetase activity, resulting in cytotoxicity specific for leukemic cells that depend on an exogenous source of the amino acid asparagine for their protein metabolism and survival.
For research use only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products
without prior written approval from Creative BioMart.
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