Recombinant Mouse TrkB Protein (His Tag)

Cat # Size Price Quantity
67070150 μg$325

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameTrkB, Neurotrophic tyrosine kinase receptor type 2, GP145-TrkB
SpeciesMouse
accession numberP15209-2
SourcesA DNA sequence encoding the extracellular domain of mouse NTRK2 (P15209-2) (Met 1-His 429) was expressed, with a C-terminal polyhistidine tag.
Molecular WeightThe secreted recombinant mouse NTRK2 consists of 409amino acids and has a calculated molecular mass of 46 KDa. The apparent molecular mass of rm NTRK2 is approximately 75-85 KDa in SDS-PAGE under reducing conditions.
Affinity TagC-His
Purity≥95% as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 1.0 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information


Neurotrophic tyrosine kinase (NTRK) receptors are a family of receptor tyrosine kinases essential for nervous system development, neuronal survival, differentiation, and synaptic plasticity. The family includes three members: NTRK1 (TrkA), NTRK2 (TrkB), and NTRK3 (TrkC). These receptors regulate neuronal growth, maintain neural connections, and support the function of sensory and central nervous system neurons. Beyond neural biology, NTRK signaling can influence cell proliferation, survival, and differentiation in other tissues.



NTRK receptors are single-pass transmembrane glycoproteins composed of an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyrosine kinase domain. Their extracellular regions contain leucine-rich repeats and immunoglobulin-like domains involved in ligand recognition and receptor interactions. Binding of a neurotrophin promotes receptor dimerization and autophosphorylation, initiating downstream signaling pathways such as RAS–MAPK, PI3K–AKT, and PLCγ. These pathways regulate gene expression, neuronal survival, differentiation, and synaptic function.



The three receptors have distinct but overlapping ligand preferences. NTRK1 primarily binds nerve growth factor (NGF), NTRK2 binds brain-derived neurotrophic factor (BDNF) and neurotrophin-4 (NT-4), and NTRK3 preferentially binds neurotrophin-3 (NT-3). Ligand specificity is not absolute, as NT-3 can activate other Trk receptors under certain conditions. Neurotrophins may also interact with the p75 neurotrophin receptor, which can modify signaling outcomes.



Altered NTRK signaling is associated with neurological conditions, including sensory and pain disorders, as well as developmental abnormalities. In cancer, chromosomal rearrangements involving NTRK genes can generate oncogenic fusion proteins that retain the kinase domain and drive constitutive signaling. These NTRK fusions occur across multiple tumor types and can promote uncontrolled cell growth and survival.



Therapeutically, selective TRK inhibitors, including larotrectinib and entrectinib, are used to treat eligible cancers harboring NTRK gene fusions. Research also explores modulation of neurotrophin–Trk signaling to support neuronal protection, regeneration, and treatment of neurological disorders.

Data Sheets


Recombinant Mouse TrkB Protein (His Tag) TDS

Frequently Asked Questions


What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.

What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.

How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.

Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.

Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

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