Recombinant Human FGF4 Protein

Beta LifeScience SKU/CAT #: BL-1648SG

Recombinant Human FGF4 Protein

Beta LifeScience SKU/CAT #: BL-1648SG
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag N/A
Host Species Human
Accession P08620
Synonym Heparin-binding growth factor 4, HBGF-4, Heparin secretory-transforming protein 1, HST, HST-1, HSTF-1, Transforming protein KS3, FGFK, KFGF, Kaposi-€™s sarcoma associated FGF
Background A member of the FGF family, FGF4 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. FGF4 binds to anionic glycosaminoglycans heparin and heparin sulfate with high affinity and mediates its diverse functions through the FGF receptors (FGFR) 1c, 2c, 3c, and 4. Human FGF4 is known to exhibit cross species activity with mouse, rat, bovine and canine FGF4. Recombinant Human FGF4 is a single polypeptide of 20 kDa.
Description Recombinant Human FGF4 was produced in E. coli. This protein is purified with our unique purification methods.
Source E.coli
Molecular Weight 20.0 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human FGF4 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis.
Subcellular Location Secreted.
Protein Families Heparin-binding growth factors family
Database References

Gene Functions References

  1. our study demonstrated that FGFR4 rs2011077 and rs1966265 are associated with the progression of cervical normal tissues to precancerous lesions in Taiwanese women. Moreover, rs351855 (Gly388Arg) is the only FGFR4 genetic polymorphism that is associated with patient survival. PMID: 28378614
  2. Thus, we conclude that the oncoprotein HBXIP up-regulates FGF4 through activating transcriptional factor Sp1 to promote the migration of breast cancer cells. Therapeutically, HBXIP may serve as a novel target in breast cancer. PMID: 26828265
  3. Fibroblasts induce expression of FGF4 in ovarian cancer stem-like cells/cancer-initiating cells and upregulate their tumor initiation capacity. PMID: 25329002
  4. Data show that the interaction between Artd1 and Sox2 is crucial for the first steps of the reprogramming process and that early expression of Fgf4 is an essential component for the successful generation of iPSCs. PMID: 23939864
  5. Myoblasts which overexpress FGF-4 exhibit significant changes in cell cycle and pro-angiogenic potential with only slight differences in the expression of the myogenic genes. PMID: 21673370
  6. In vivo stimulation of BT-474 cell growth by progesterone is associated with up-regulation of FGF4 which may promote tumor growth and maintenance. PMID: 22237711
  7. knockdown of FGFR4 expression led to decreased proliferation and an increased rate of apoptosis in the MKN45 and SGC7901 GC cell lines PMID: 21567388
  8. activation of human HST-1 gene in transgenic mice induces spermatogenesis and prevents adriamycin-induced testicular toxicity PMID: 11840335
  9. Differential effects of FGF4, EGF and TGFB1 on functional development of stromal layers (progenitor cell-outputs) in acute myeloid leukemia PMID: 12163055
  10. FGF4 is upregulated by the OCT3 transcription factor in breast cancer cells. PMID: 12841847
  11. HST-1 protects male germ cells from apoptosis under heat-stress condition in a mouse model. PMID: 14980503
  12. Both myeov and hst (fgf4) are normally situated approximately 475-kb apart at band 11q13, a region that is frequently amplified and overexpressed in various tumours. PMID: 17390055
  13. FGF-4 increases the rate at which MSC proliferate and has no significant effect on MSC pluripotency PMID: 17852409
  14. These results suggest a growth-promoting role for FGF4 in human embryonic stem cells and a putative feedback inhibition mechanism by a novel FGF4 splice isoform that may serve to promote differentiation at later stages of development. PMID: 18192227
  15. Implantation of human FGF4-soaked beads is sufficient to restore expression of G1- and S-phase cell-cycle genes and S-phase progression in zebrafish sonic hedgehog (Shh) mutant fin buds. PMID: 18811955
  16. The combined action of retinoic acid and FGF4 results in induction of PDX1+ foregut endoderm. PMID: 19277121

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.

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