Recombinant Human FGFR4 Protein (His Tag)

Name: Recombinant Human FGFR4 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2079
Availability: InStock

Collections: Cytokines and growth factors, Enzymes, Growth factors and receptors, Kinase, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_002002.3
Synonym	FGFR4, CD334, JTK2, TKF, fibroblast growth factor receptor 4
Background	Fibroblast growth factor receptor 4 is a protein that in humans is encoded by the FGFR4 gene. FGFR4 has also been designated as CD334 (cluster of differentiation 334).FGFR4 (Fibroblast Growth Factor Receptor 4) is a Protein Coding gene. Diseases associated with FGFR4 include Prostate Cancer and Rhabdomyosarcoma. Among its related pathways are PI3K/AKT activation and RET signaling. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring phosphorus-containing groups and protein tyrosine kinase activity. An important paralog of this gene is FGFR3.
Description	A DNA sequence encoding the extracellular domain (Met 1-Asp 369) of human FGFR4 (NP_002002.3) was fused with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Leu 22
AA Sequence	Met 1-Asp 369
Molecular Weight	The secreted recombinant human FGFR4 consists of 359 amino acids and has a predicted molecular mass of 40 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh FGFR4 is approximately 60 kDa due to glycosylation.
Purity	>97% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its ability to inhibit FGF acidic (aFGF / FGF1) dependent proliferation of Balb/c3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.2-1ug/mL.
Formulation	Recombinant Human FGFR4 Protein (His Tag) was lyophilized from sterile PBS, pH 7.4
Stability	Recombinant Human FGFR4 protein is stable up to 1 year at -70°C
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.