Abcam, ab34616, Biotin Anti-Asparaginase antibody

Size: 100µg
Rabbit Polyclonal ASPG2 antibody - conjugated to Biotin. Suitable for ELISA, WB and reacts with Escherichia coli samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Conjugation:Biotin,
Carrier free:No,
Reacts with:Escherichia coli,
Applications:ELISA, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Purification technique-Ion exchange chromatography, Purification notes-Anti-L-Asparaginase is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer., Storage buffer-Preservative: 0.01% Sodium azideConstituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Asparaginase commonly known as L-asparaginase is an enzyme that catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. This enzyme is present in various organisms including bacteria such as Escherichia coli. It is often produced using recombinant methods in strains like E. coli as L-asparaginase or trade names like aspergcel. The molecular mass of L-asparaginase is approximately 135 kDa. It is primarily expressed in microbial cells but is also significant in commercial and medical applications for its enzymatic properties.
Biological function summary
This enzyme plays an important role in the metabolism of amino acids. Unlike humans and some tumor cells normal cells can synthesize L-asparagine while certain types of cancer cells lack this ability and depend on external sources. This dependency makes L-asparaginase an effective therapeutic enzyme as it depletes circulating L-asparagine inhibiting protein synthesis in such tumor cells. The enzyme functions independently and does not typically combine into complex structures.
Pathways
L-asparaginase is involved in the asparagine degradation pathway. This pathway impacts protein synthesis and nitrogen metabolism. When applied therapeutically it interacts indirectly with protein synthesis pathways by reducing the availability of asparagine for cells that cannot synthesize it. Additionally when pegylated PEG-asparaginase it displays enhanced stability and a prolonged circulating half-life providing an efficient effect on target pathways.
Asparaginase is prominently linked to the treatment of acute lymphoblastic leukemia (ALL). Its mechanism to lower asparagine levels starves leukemia cells of necessary nutrients leading to apoptosis. The enzyme is also studied for its potential effects in certain solid tumors that express deficiencies in asparagine synthetase a related protein. Moreover levels of asparaginase activity are often monitored via specialized assays to ensure therapeutic efficacy and manage side effects during treatment.