Recombinant Human FGF3 Protein

Beta LifeScience SKU/CAT #: BL-1647SG

Recombinant Human FGF3 Protein

Beta LifeScience SKU/CAT #: BL-1647SG
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Product Overview

Tag N/A
Host Species Human
Accession P11487
Synonym HBGF-3, FGF3, Proto-oncogene Int-2, Heparin-binding growth factor 3
Background FGF3 belongs to the FGF family, members of which act on cells of mesodermal and neuroectodermal origin. Originally designated int2, the FGF3 gene was initially identified as a protooncogene in mice. FGF3 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation and is required for normal ear development. Heparan sulfate glycosaminoglycans function as co-receptors to increase the affinity between FGF3 and its receptors; FGFR1 and FGFR2. Human and mouse FGF3 are known to share 88% amino acid sequence identity. Recombinant Human FGF3 is a single polypeptide of 21 kDa.
Description Recombinant Human FGF3 was produced in E. coli. This protein is purified with our unique purification methods.
Source E.coli
Molecular Weight 21.2 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 FGF3 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 ear development.
Subcellular Location Secreted.
Protein Families Heparin-binding growth factors family
Database References
Associated Diseases Deafness with labyrinthine aplasia, microtia and microdontia (LAMM)

Gene Functions References

  1. FGFR1 and/or FGF3 gene amplification correlated with a lower pathologic complete response in patients with HER2(+) early breast cancer treated with neoadjuvant anti-HER2 therapy PMID: 28381415
  2. fibroblast growth factor receptor 3 missense mutations were identified in 5 cases of thanatophoric dysplasia PMID: 28249712
  3. MCF7 cells over-expressing both WNT1 and FGF3 show a 3.5-fold increase in mammosphere formation; conditioned media from these cells also promotes stem cell activity in untransfected parental MCF7 and T47D cells, as WNT1 and FGF3 are secreted factors. PMID: 26421711
  4. analysis provided evidence for gene-gene interaction between FGF3 (rs4980700) and PAX9 (rs2073242), increasing risk for isolated oral clefts (p = 0.0003). FGF3 is associated with oral clefts and may interact with PAX9. PMID: 24697712
  5. haplotypes may contribute to the tendon disease process in elite volleyball athletes PMID: 24661680
  6. FGF3 gene expression is altered in a human breast cancer progression model. PMID: 25333703
  7. Higher FGF-23 concentration was associated with LVED mass and with incident atrial fibrillation and may, in part, explain the link between chronic kidney disease and AF. PMID: 24920722
  8. A de novo 290 kb interstitial duplication of chromosome 11q13.3 including the FGF3 and FGF4 genes. PMID: 24120895
  9. tooth agenesis had increased risk of a family history of cancer. tooth agenesis was associated with positive self-reported family history of cancer and variants in FGF3. PMID: 23169889
  10. This study is the first to show a significant association between coronary calcification and elevated serum FGF 23 in children. PMID: 21359960
  11. confirm the absence of otodental syndrome in heterozygous FGF3 carriers, but report unilateral microtia in one of them PMID: 21480479
  12. Manifestations of recessive FGF3 mutations range from fully penetrant LAMM syndrome to deafness with residual inner ear structures and, by extension, with minimal syndromic features. PMID: 21306635
  13. alterations in dosage of the Fgf3 gene cause dental morphological changes PMID: 20018768
  14. labyrinth aplasia, microtia, and microdontia (LAMM) syndrome, caused by mutations in FGF3 PMID: 19950373
  15. These findings suggest that the nuclear form of FGF3 inhibits cell proliferation by interfering with ribosomal biogenesis. PMID: 16263090
  16. Development of the inner ear is completely disturbed at a very early stage--or the otic vesicle is not induced at all--in all of the affected individuals who carried two mutant FGF3 alleles PMID: 17236138
  17. FGF3, FGF7, FGF10, FGF18, and FGFR1 may have roles in nonsyndromic cleft lip and palate PMID: 17360555
  18. Implication of FGF3 and FADD in human craniofacial disease. PMID: 17656375
  19. sequenced the FGF3 gene in 10 unrelated families in which probands had congenital deafness associated with various inner ear anomalies, including Michel aplasia, with or without tooth or external ear anomalies. PMID: 18435799
  20. study identified a homozygous missense mutation (c.196G-->T) in FGF3 in 21 affected individuals from a large extended family phenotypically characterized by autosomal recessive syndromic congenital sensorineural deafness, microtia and microdontia PMID: 18701883
  21. Loss of FGFR3 signaling provides evidence that extracellular signals regulate not simply the proliferation or survival of radial glial cells, but specifically their progression to intermediate progenitor cells during neurogenesis in vivo. PMID: 19923290

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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