Recombinant Human FGF8 Protein

Name: Recombinant Human FGF8 Protein
Brand: Beta LifeScience
SKU: BL-2233PS
Availability: InStock

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

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Product Overview

Tag	N/A
Host Species	Human
Synonym	FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Background	FGF8 is part of the fibroblast growth factor family. FGFfamily members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Description	FGF8 Human Recombinant expressed in E.Coli is a non-glycosylated polypeptide chain containing 194a.a. and having a total molecular weight of 22.5kDa.
Source	E.coli
AA Sequence	MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.
Purity	>97.0% as determined by analysis by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Bioactivity	The ED50, as determined by its ability to induce proliferation of mouse 3T3 fibroblasts, is 5-7ng/ml, corresponding to a specific activity of 2x105units/mg.
Formulation	Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50mM NaCl, pH 7.5.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Lyophilized FGF8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF8 should be stored at 4?C between 2-7 days and for future use below -18?C.

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.