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膀胱癌腫瘤標誌物檢測試劑盒Urinary Bladder Neoplasms Molecular Marker Detection Kit
[編輯]膀胱癌腫瘤分子標誌物檢測試劑盒 Urinary Bladder Neoplasms Molecular Marker Detection Kit
[Source: http://www.biopharmsoft.com]
Description: The kit provides a means of performing Urinary Bladder Neoplasms detection method based on kinase activity assay. This kit includes Streptavidin Coated Plates and specific SubstratePeptides (biotinylated peptide substrates) for detection of the activity of EGFR, FGFR3 and SRC which indicate the prognosis of Urinary Bladder Neoplasms.
Label of Substrate-Peptides: Biotinylated.
Quality Control: The substrate peptide was selected using our Urinary Bladder Neoplasms Diagnosis Kit. The quality of the biotinylated peptide was evaluated by reverse-phase HPLC and by mass spectrometry.
Storage:
Store at 4 °C, Avoid Freeze.
Background:
EGFR (epidermal growth factor receptor) exists on the cell surface and is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor α (TGFα) (note, a full list of the ligands able to activate EGFR and other members of the ErbB family is given in the ErbB article). ErbB2 has no known direct activating ligand, and may be in an activated state constitutively or become active upon heterodimerization with other family members such as EGFR. Upon activation by its growth factor ligands, EGFR undergoes a transition from an inactive monomeric form to an active homodimer – although there is some evidence that preformed inactive dimers may also exist before ligand binding. FGFR3 is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. Src (pronounced "sarc" as it is short for sarcoma) is a proto-oncogene encoding a tyrosine kinase originally discovered by J. Michael Bishop and Harold E. Varmus, for which they won the 1989 Nobel Prize in Physiology or Medicine. It belongs to a family of non-receptor tyrosine kinases called Src family kinases. The discovery of Src family proteins has been instrumental to the modern understanding of cancer as a disease where normally healthy cellular signalling has gone awry.