Recombinant Human TrkA
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BackgroundThe Trk proto-oncogene family contains four members, TrkA, TrkB, TrkC and TrkE, which are members of the neurotropic tyrosine kinase receptor family. They are variably expressed throughout the central and peripheral nervous systems. TrkA binds to nerve growth factor (NGF) and autophosphorylates to activate multiple downstream effector proteins (1-2). Phosphorylation of TrkA is required for Shc association and subsequent activation of the Ras-MAP kinase-signaling cascade, which leads to activation of Elk-1-dependent gene transcription and neurite growth (3). Also, phosphorylation is required for PI3-kinase association and activation of the Akt signaling cascade. The presence of TrkA leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in this gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation and cancer. Expression of Trk receptors also plays an important role in the biology and clinical behavior of neuroblastomas. High expression of TrkA is present in neuroblastomas with favorable biological features and highly correlated with patient survival, whereas TrkB is mainly expressed on unfavorable, aggressive neuroblastomas (4). Protein DetailsPurity >95% by SDS-PAGE and analyzed by silver stain. Endotoxin Level <0.01EU/µg as determined by the LAL method ⋅ <1.0 EU/µg as determined by the LAL method Biological Activity The biological activity of Human TrkA was determined by its ability to inhibit NGF-induced proliferation of TF1 cells. The ED50 for this effect is typically 0.8 - 4 μg/ml in the presence of 10 ng/ml of rhNGF. Fusion Protein Tag Fc Fusion Protein Protein Accession No. Amino Acid Sequence aapcpdac cphgssglrc trdgaldslh hlpgaenlte lyienqqhlq hlelrdlrgl gelrnltivk sglrfvapda fhftprlsrl nlsfnalesl swktvqglsl qelvlsgnpl hcscalrwlq rweeeglggv peqklqchgq gplahmpnas cgvptlkvqv pnasvdvgdd vllrcqvegr gleqagwilt eleqsatvmk sgglpslglt lanvtsdlnr knltcwaend vgraevsvqv nvsfpasvql htavemhhws ipfsvdgqpa pslrwlfngs vlnetsfift eflepaanet vrhgclrlnq pthvnngnyt llaanpfgqa sasimaafmd npfefnpedp ipdtnstsgd pvekkdeieg ridpkscdkt htcppcpape llggpsvflf ppkpkdtlmi srtpevtcvv vdvshedpev kfnwyvdgve vhnaktkpre eqynstyrvv svltvlhqdw lngkeykckv snkalpapie ktiskakgqp repqvytlpp srdeltknqv sltclvkgfy psdiavewes ngqpennykt tppvldsdgs fflyskltvd ksrwqqgnvf scsvmhealh nhytqkslsl spgk
N-terminal Sequence Analysis Ala33 State of Matter Lyophilized Predicted Molecular Mass The predicted molecular weight of Recombinant Human is Mr 67.4 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 115-125 kDa. Predicted Molecular Mass 67.4 Formulation This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.
Storage and Stability This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions. Country of Origin USA Shipping Next Day Ambient NCBI Gene Bank References & Citations1. Esposito, D. et al. (2001) J. Biol. Chem. 276:32687 2. Sofroniew, MV. et al. (2001) Annu. Rev. Neurosci. 24:1217 3. Gu, H. et al. (2000) Mol. Cell. Biol. 20:7109 4. Eggert, A. et al. (2005) Cancer Lett. 228:143 Certificate of AnalysisIMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein. |
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Products are for research use only. Not for use in diagnostic or therapeutic procedures.