Canine TrkA/NTRK1 (His Tag) recombinant protein

Canine TrkA/NTRK1 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding to nerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.

TRK1; TRK; TKR; MTC; DKFZP781I14186; P140-TRKA; NTRK1; C80751; TRKA; TRK-A

Human Cells

A DNA sequence encoding the canine NTRK1 (XP_851619.3) (Pro285-Lys410) was expressed with a N-terminal polyhistidine tag.

Canine

The recombinant canine NTRK1 comprises 146 amino acids and has a predicted molecular mass of 16.2 kDa. The apparent molecular mass of the protein is approximately 27-33 kDa in SDS-PAGE under reducing conditions due to glycosylation.

> 95 % as determined by SDS-PAGE

Measured by its ability to inhibit NGF-induced proliferation of TF‑1 human erythroleukemic cells.
The ED₅₀ for this effect is typically 3-24 µg/mL in the presence of 10 ng/mL of recombinant human NGF.