MyBioSource.com's Cyclic nucleotidase is a Rabbit Polyclonal antibody. This antibody has been shown to work in applications such as: Immunoprecipitation, and Western Blot.
Description
Various cytotoxic nucleoside analogs (NA) have been employed in the treatment of hematologic malignancies. These NA include pyrimidine analog cytosine arabinoside (ara-c) and purine analogs, cladribine and fludarabine. These NA become therapeutically effective only after phosporylation to the triphosphate level. The 5'-nucleotidases (5'-NTs) dephosphorylate the monophosphate form of NA and, therefore, may affect the pharmacological activity of these antimetabolites. Several 5'-NTs attached to membranes or present in the cytosol or in mitochondri. There are two cytosolic cyclic 5'nucleotidases are cN-II and dNT-1 and one mitochondrial (dNT-2) nucleotidase known to be present in the cells. cN-I plays a significant role in AMP breakdown to adenosine whereas cN-II breaks down IMP to inosine and GMP to guanosine. The primary sequence of CNI is unrelated to CNII or ecto-5'nucleotisdase (e-N). The tissue distribution of cNI cNII is different, cNI is found only in vertebrate heart where as cNII is expressed in heart, brain and muscle. Sequence alignments of cytosolic 5'-nucleotidase, along with other nucleotidases, suggest that cytosolic 5'nucleotidase belong to a large superfamily of hydrolases with different substrate specificities and functional roles. Overproduction of cN-II could lead to resistance against anti-cancer drugs based on purine analogs. cN-II is Mg2+- dependent, regulated and stabilized by several factors such as allosteric effectors ATP and 2,3-DPG, although these are not directly involved in the reaction stoichiometry (2). IMP and GMP and its derivatives specific cytosolic 5'-nucleotidase (cNII) acts through the formation of a phosphoenzyme intermediate. Phosphate either released leading to 5'-mononucleotide hydrolysis or transferred to an appropriate nucleoside acceptor, giving rise to a mononucleotide interconversion. Chemical reagents specifically modifying aspartate and glutamate residues inhibit the enzyme, and this inhibition is partially prevented by cN-II substrates and physiological inhibitors (3). Site-directed mutagenesis experiments confirmed the essential role of Asp-52 in the catalytic machinery of the enzyme and suggested also that Asp-54 assists in the formation of the acyl phosphate species. There exist a putative phsohorylation site on the cNII near C-termianl end of the protein. MyBioSource has also produced a phsopho-specific antibody to phospho-serine residue at this site (phosphorylation site: ILFRSG(Sp)RQTLES). The CNII exist as monomer (40 kDa) and multimeric forms in various tissues. Anti-CNII-selective antibodies were generated using unique peptide from the CNII protein. The antibody CNII-101AP has unique epitope that is present on cNII and not on cNI or e-N type of nucleotidases. The affinity purified version of this antibody (cNII-101AP) was isolated form immobilized antigen based affinity chromatography and are represented as pure IgG fractions stabilized in antibody stabilization buffer. The mono-epitope specific polyclonal antibody (cNII-101AP) strongly label a 40-42 kDa cNII and its multimerric forms in PC-cNII samples. A phospho-specific antibody to cNII is also available form MyBioSource. The cNII antibodies can be conjugated as HRP or alkaline conjugates for IHC, Confocal, WB analyses at a nominal fee. MyBioSource will also conjugate antibodies with fluorescent probes upon request at extra charge