Anti-AMV Monoclonal antibody (DMAB9357)
Mouse Anti-AMV Monoclonal antibody for IP, WB, IHC
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Avian myeloblastosis virus from Avian Myeloblastosis Virus, grown in chickens, purified by sucrose gradient and ether extracted.
Avian Myeloblastosis Virus; AMV
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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PRESS, RD; KIM, A; et al. TRANSFORMATION OF CHICKEN MYELOMONOCYTIC CELLS BY A RETROVIRUS EXPRESSING THE V-MYB ONCOGENE FROM THE LONG TERMINAL REPEATS OF AVIAN-MYELOBLASTOSIS VIRUS BUT NOT ROUS-SARCOMA VIRUS. JOURNAL OF VIROLOGY 66:5373-5383(1992).
Butt, AM; Duncan, A; et al. Cells expressing the NG2 antigen contact nodes of Ranvier in adult CNS white matter. GLIA 26:84-91(1999).
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody.