The ALK Antibody Sampler Kit provides an economical means of detecting total ALK as well as ALK phosphorylated at various residues. The kit includes enough antibody to perform four western blot experiments with each primary antibody.
ALK (C26G7) Rabbit mAb detects endogenous levels of total ALK protein. This antibody does not cross-react with other family members. Each activation state antibody recognizes only its specific target. Slight cross-reactivity with over expressed receptor tyrosine kinases may occur.
Monoclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1078, Tyr1096, Tyr1278, Tyr1282/1283, or Tyr1586 of human ALK protein, or a recombinant fusion protein surrounding amino acid 1475 of human ALK protein. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1278/1282/1283 or Tyr1604 of human ALK protein. Antibodies are purified by protein A and peptide affinity chromatography.
Anaplastic lymphoma kinase (ALK) is a tyrosine kinase receptor for pleiotrophin (PTN), a growth factor involved in embryonic brain development (1-3). In ALK-expressing cells, PTN induces phosphorylation of both ALK and the downstream effectors IRS-1, Shc, PLCγ, and PI3 kinase (1). ALK was originally discovered as a nucleophosmin (NPM)-ALK fusion protein produced by a translocation (4). Investigators have found that the NPM-ALK fusion protein is a constitutively active, oncogenic tyrosine kinase associated with anaplastic lymphoma (4). Research literature suggests that activation of PLCγ by NPM-ALK may be a crucial step for its mitogenic activity and involved in the pathogenesis of anaplastic lymphomas (5).
A distinct ALK oncogenic fusion protein involving ALK and echinoderm microtubule-associated protein like 4 (EML4) has been described in the research literature from a non-small cell lung cancer (NSCLC) cell line, with corresponding fusion transcripts present in some cases of lung adenocarcinoma. The short, amino-terminal region of the microtubule-associated protein EML4 is fused to the kinase domain of ALK (6-8).
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