TrkA Protein, Human (HEK293, His-Fc)

TrkA protein is an important receptor tyrosine kinase that regulates the development of the central and peripheral nervous systems and affects the proliferation, differentiation, and survival of neurons. As a high-affinity receptor for NGF, TrkA is activated upon NGF binding through homodimerization and autophosphorylation. TrkA Protein, Human (HEK293, His-Fc) is the recombinant human-derived TrkA protein, expressed by HEK293 , with C-hFc, C-His labeled tag. The total length of TrkA Protein, Human (HEK293, His-Fc) is 382 a.a., with molecular weight of 85-95 kDa.

TrkA Protein, a receptor tyrosine kinase, plays a crucial role in the development and maturation of both the central and peripheral nervous systems, exerting control over the proliferation, differentiation, and survival of sympathetic and sensory neurons. Functioning as a high-affinity receptor for NGF, its primary ligand, TrkA undergoes homodimerization, autophosphorylation, and activation upon dimeric NGF ligand-binding. This activation leads to the recruitment, phosphorylation, and/or activation of downstream effectors, including SHC1, FRS2, SH2B1, SH2B2, and PLCG1, orchestrating distinct signaling cascades that drive cell survival and differentiation. TrkA regulates diverse cellular processes through pathways such as the GRB2-Ras-MAPK cascade, Ras-PI3 kinase-AKT1 signaling, and NF-Kappa-B activation. In the absence of ligand and activation, TrkA may contribute to cell death, emphasizing the dependence of neuron survival on trophic factors. Interestingly, it exhibits resistance to NGF, constitutively activating AKT1 and NF-kappa-B, while unable to activate the Ras-MAPK signaling cascade. TrkA also antagonizes the anti-proliferative NGF-NTRK1 signaling, promoting neuronal precursor differentiation. The isoform TrkA-III additionally plays a role in angiogenesis and exhibits oncogenic activity upon overexpression.

Human

HEK293

C-hFc;C-His

P04629 (M1-P382)

4914  [NCBI]

85-95 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.