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Polyclonal Antibody Immunoprecipitation Neural Crest Cell Migration

$303
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Ret proto-oncogene (c-Ret) is a receptor tyrosine kinase that functions as a multicomponent receptor complex in conjunction with other membrane-bound, ligand-binding GDNF family receptors (1). Ligands that bind the Ret receptor include the glial cell line-derived neurotrophic factor (GDNF) and its congeners neurturin, persephin, and artemin (2-4). Research studies have shown that alterations in the corresponding RET gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma, and a congenital developmental disorder known as Hirschsprung’s disease (1,3). The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr at position 905 dramatically inhibits Ret autophosphorylation activity (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Ret proto-oncogene (c-Ret) is a receptor tyrosine kinase that functions as a multicomponent receptor complex in conjunction with other membrane-bound, ligand-binding GDNF family receptors (1). Ligands that bind the Ret receptor include the glial cell line-derived neurotrophic factor (GDNF) and its congeners neurturin, persephin, and artemin (2-4). Research studies have shown that alterations in the corresponding RET gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma, and a congenital developmental disorder known as Hirschsprung’s disease (1,3). The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr at position 905 dramatically inhibits Ret autophosphorylation activity (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Secreted Frizzled-related proteins (SFRPs) display homology and structural similarity to the extracellular cysteine-rich Wnt-binding domain of the G protein-coupled receptor Frizzled (1,2). To date, five distinct SFRPs (SFRP1 to 5) have been found in mammalian cells. These secreted proteins typically act as antagonists to Wnt signaling by directly binding and inhibiting Wnt proteins, or by binding Frizzled to block Wnt protein interaction with the receptor (3). The various SFRPs bind and regulate Wnt proteins differentially; these proteins also display distinct expression patterns as they play important roles in regulating development (4-7). SFRP proteins appear to act as tumor suppressors, with loss of expression or function correlating with many invasive forms of cancer. Deletion of the corresponding SFRP1 gene and promoter hypermethylation leading to gene silencing has been reported in a number of cancers. Abnormal expression of SRFP1 and other Wnt signaling proteins is associated with some cases of retinitis pigmentosa (reviewed in 8).