Mouse GFRA2 / GFRα2 / GDNFRB Protein (His Tag)

Mouse GDNF Family Receptor Alpha-2 Protein

GFRA2 / GDNFRB / GFR-alpha-2 Protein Product Information

• Synonym: Gfra2 , GFR alpha 2 , GFR alpha-2
• Protein Construction: A DNA sequence encoding the mouse GFRα2 (NP_032141.2) (Met 1-Ser 441) without the propeptide was expressed, fused with a polyhistidine tag at the C-terminus
• Source: Mouse
• Expression Host: Human Cells

GFRA2 / GDNFRB / GFR-alpha-2 Protein QC Testing

• Purity: > 85 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ser 22
• Molecular Mass: The secreted recombinant mouse GFRα2 consists of 431 amino acids and has a calculated molecular mass of 48.5 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 75kDa band in SDS-PAGE under reducing conditions
• Formulation: Lyophilized from sterile PBS , pH 7.4
• SDS-PAGE: GFRA2 protein

GFRA2 / GDNFRB / GFR-alpha-2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

GFRA2 / GDNFRB / GFR-alpha-2 Protein Description

Mouse GDNF family receptor alpha-2, also known as GFR-alpha-2, Neurturin receptor alpha, TGF-beta-related neurotrophic factor receptor 2, GFRA2, GFRα-2, and GDNFRB, is a cell membrane protein which belongs to the GDNFR family. Glial cell line-derived neurotrophic factor (GDNF) and neurturin (NTN) are two structurally related, potent neurotrophic factors that play key roles in the control of neuron survival and differentiation. GDNF is a glycosylated, disulfide-bonded homodimer that is distantly related to the TGF-beta superfamily of growth factors. Three receptors for these factors, GFRα-1, GFRα-2 and GFRα-3 have been identified. These receptors do not contain transmembrane domains and are attached to the cell membrane by GPI linkage. Both GFRα-1 and GFRα-2 have been shown to mediate the GDNF-dependent and NTN-dependent phosphorylation and activation of the tyrosine kinase Ret which is necessary for kidney and enteric neuron development. GFRα-1 is the primary receptor for GDNF and GFRα-2 exhibits a preference for NTN. GFRα-2 mediates the NRTN-induced autophosphorylation and activation of the RET receptor. It can also mediate GDNF signaling through the RET tyrosine kinase receptor.

References

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