Anti-AMV Monoclonal antibody (DMAB9357)

Mouse Anti-AMV Monoclonal antibody for IP, WB, IHC Datasheet

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Host Species
Antibody Isotype
Species Reactivity
Avian myeloblastosis virus from Avian Myeloblastosis Virus, grown in chickens, purified by sucrose gradient and ether extracted.


Alternative Names
Avian Myeloblastosis Virus; AMV

Product Background

Antigen Description
AMV reverse transcriptase synthesizes DNA complementary (cDNA) to RNA templates. A DNA primer complementary to the RNA template and a divalent cation, either Mg or Mn, are required for initiation of transcription. This enzyme is commonly used to make cDNAs from mRNA for eventual cloning or for use as probes. The four major internal structural proteins (the group-specific antigens) of avian myeloblastosis virus are formed by sequential cleavage of a precursor polypeptide with Mr = 76,000 (Pr76). The evidence for this conclusion is based on analysis of immune precipitates from lysates of AMV§-infected cells treated with a multivalent antiserum directed against these proteins. Sodium dodecyl sulfate gel electrophoresis of such immune precipitates from cells pulse-labeled with [35S]-methionine reveals five metabolically unstable radioactive polypeptides. These polypeptides behave kinetically as precursors to virion proteins. Double-label ion-exchange chromatography of tryptic digests of the unstable polypeptides demonstrates that the largest precursor, Pr76, contains the amino acid sequences of all four virion proteins. It appears not to contain the sequence of the fifth and smallest internal virion protein. The four smaller precursors are intermediate cleavage products of Pr76. The arrangement of the virion proteins in Pr76 was determined by labeling cells shortly after inhibiting polypeptide chain initiation. The relative amounts of radioactivity both in completed virion proteins and in the tryptic peptides of Pr76 implies the same order for three of the four proteins. The exact position of one protein remains uncertain. On the basis of these experiments, we propose a cleavage pathway for the generation of the structural proteins of AMV. We also demonstrate that cleavage of precursors can proceed in crude extracts of AMV-infected cells. This proteolysis, while resistant to several protease inhibitors, is completely blocked by addition of agents that disrupt membranes.


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Hamilton, RI; et al. Legume virus research in Canada: A retrospective and a view of the future. CANADIAN JOURNAL OF PLANT PATHOLOGY-REVUE CANADIENNE DE PHYTOPATHOLOGIE 19:208-214(1997).
Fu, SL; Lipsick, JS; et al. FAETL motif required for leukemic transformation by v-Myb. JOURNAL OF VIROLOGY 70:5600-5610(1996).

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