Recombinant Human Fibroblast Growth Factor 8 (FGF8), Active

Name: Recombinant Human Fibroblast Growth Factor 8 (FGF8), Active
Brand: Beta LifeScience
SKU: BLC-05931P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Buy cytokines, chemokines, and growth factors for research online, Explore high-quality enzymes for research and supplementation, Featured enzyme molecules, Growth factors and receptors for advanced research, High-quality cytokines for advanced research, High-quality recombinant proteins, Kinase

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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Fibroblast Growth Factor 8 (FGF8), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a cell proliferation assay using BALB/c 3T3 cells is less than 100 ng/ml.
Uniprotkb	P55075
Target Symbol	FGF8
Synonyms	AIGF; Androgen induced growth factor; Androgen-induced growth factor; FGF 8; FGF-8; FGF-8b; FGF8; FGF8_HUMAN; Fibroblast growth factor 8 (androgen induced); Fibroblast growth factor 8; Fibroblast growth factor 8 precursor; HBGF 8; HBGF-8; HBGF8; Heparin-binding growth factor 8; HH6; KAL6
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	QVTVQSSPNFTQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR
Expression Range	23-215aa
Protein Length	Partial of Isoform 3
Mol. Weight	22.5 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells.
Subcellular Location	Secreted.
Protein Families	Heparin-binding growth factors family
Database References	HGNC: 3686 OMIM: 600483 KEGG: hsa:2253 STRING: 9606.ENSP00000321797 UniGene: PMID: 30079292 Study demonstrated that FGF8 can regulate germ cell fate by modulating the dynamic equilibrium between differentiation and self-renewal. PMID: 28898437 FGF8 and FGFR3 may therefore play an important role in the onset of deep zone necrosis and pathogenesis in Kashin-Beck disease in adolescent children. PMID: 29626475 we also found that FGF8 increased the expression of YAP1 and knockdown of YAP1 eliminated the upregulation of EGFR and the resistance to EGFR inhibition induced by FGF8. Our study provides evidence that FGF8 plays an important role in the resistance to EGFR inhibition of human hepatocellular carcinoma cells PMID: 28791365 Genetic testing identified a de novo, heterozygous mutation in fibroblast growth factor receptor 1 (FGFR1 p.L630P). L630 resides on the ATP binding cleft of the FGFR1 tyrosine kinase domain, and L630P is predicted to cause a complete loss of receptor function. Cell-based assays confirmed that L630P abolishes FGF8 signaling activity PMID: 28195315 Bonferroni adjusted p-value: 0.04). No statistically significant associations were identified in the other ethnic groups. In conclusion, variant/s in FGF2 and FGF8 may predispose diabetics with CKD to LEA. PMID: 27237708 in one holoprosencephaly (HPE) family, a deleterious FGFR1 allele was transmitted from one parent and a loss-of-function allele in FGF8 from the other parent to both affected daughters. This family is one of the clearest examples to date of gene:gene synergistic interactions causing HPE in humans. PMID: 26931467 Fgf8 activates Ras-ERK pathway to specify hindbrain. Downstream of ERK, Pea3 specifies isthmus (rhombomere 0, r0), and Irx2 may specify r1, where the cerebellum is formed. PMID: 27273073 Regulation of neurogenesis by Fgf8a requires Cdc42 signaling and a novel Cdc42 effector protein PMID: 23994638 Our results link FGF8, c-Abl and p300 in a regulatory pathway that controls DeltaNp63alpha protein stability and transcriptional activity. PMID: 25911675 Data indicate that overexpression of fibroblast growth factor 8 (FGF8) correlates with lymph node metastasis and poor prognosis in colorectal cancer (CRC). PMID: 25473897 FGF8 mutations (p.Gly29_Arg34dup and p.Pro26Leu) contribute to the formation of the VATER/VACTERL association. PMID: 25131394 Scube3 may be a critical upstream regulator of fast fiber myogenesis by modulating fgf8 signaling during zebrafish embryogenesis PMID: 24849601 Together, these data demonstrate that FGF (FGFR-2 and Fgf8)signaling regulates cell proliferation and cell polarity and that these cell processes contribute to facial morphogenesis. PMID: 23906837 The oncoprotein HBXIP enhances angiogenesis and growth of breast cancer through modulating FGF8 and VEGF. PMID: 24464787 genetic association study in population in Massachusetts: Data suggest that clinical features in Kallmann syndrome (KS) are associated with genetic causes: dental agenesis/digital bony abnormalities are associated with variations/mutations in FGF8. PMID: 23533228 A novel FGF8b-binding peptide with anti-tumor effect on prostate cancer. PMID: 23466786 The results suggest that prolonged and enhanced human fibroblast growth factor 8b signaling induces dramatic changes in the epididymis and testis that lead to infertility in a portion of the human fibroblast growth factor 8b transgenic male mice. PMID: 22423049 genetic association studies in 103 patients from US and UK: Mutations in FGF8, FGFR1, or PROKR2 contributed to 7.8% of patients with combined pituitary hormone deficiency or septo-optic dysplasia. Data suggest genetic overlap with Kallmann syndrome. PMID: 22319038 In vivo stimulation of BT-474 cell growth by progesterone is associated with down-regulation of FGF-8. PMID: 22237711 We implicate FGF8 in the etiology of recessive holoprosencephaly and potentially septo-optic dysplasia/Moebius syndrome PMID: 21832120 This novel mechanism of viral-mediated FGF8 upregulation may implicate a new role of oncoviruses in human carcinogenesis. PMID: 21119603 FGF8, FGF17, and FGF18 are involved in autocrine and paracrine signaling in HCC and enhance the survival of tumor cells under stress conditions, malignant behavior, and neoangiogenesis. PMID: 21319186 FGF8b is able to induce fast growth in strongly hypoxic tumour microenvironment whereas VEGF-stimulated growth advantage is associated with improved perfusion and oxygenation of prostate tumour xenografts PMID: 21034500 Results suggest that increased FGF-8 in human prostate may also contribute to prostate tumorigenesis by stromal activation. PMID: 21076617 We identified the first nonsense mutations in the FGF8 gene in familial isolated hypogonadotropic hypogonadism with variable degrees of GnRH deficiency and olfactory phenotypes, confirming that loss-of-function mutations in FGF8 cause GnRH deficiency. PMID: 20463092 widespread expression pattern suggests FGF8 has physiological roles in adult tissue as well as in development PMID: 11953856 Promoter of FGF8 reveals a unique regulation by unliganded RARalpha. PMID: 12054865 Regulation of FGF8 expression by the androgen receptor in human prostate cancer. PMID: 12140757 isoform b isoform expressed in prostate cancer, and is of prognostic value PMID: 12778074 Repression of fgf8 might be directly or indirectly involved in this transcriptional control by TGF-beta. PMID: 15935652 We also show that the mode of FGF8 receptor-binding specificity is distinct from that of other FGFs and provide the first biochemical evidence for a physiological FGF8b-FGFR1c interaction during mid-hindbrain development. PMID: 16384934 novel role for nuclear factor-kappaB in the regulation of fibroblast growth factor 8(FGF8) expression in prostate cancer cells is uncovered PMID: 16683270 These results indicate that mutations are rare in FGF8 and FGFR2 in hypospadias, but gene variants may influence the risk. PMID: 17264867 FGF8 has a role in regulation of autocrine and paracrine loops in the growth regulation of breast, prostate and ovarian cancer [review] PMID: 17512240 Fgf8 is required for the node to impart left-right asymmetry on specific tissues Excess Fgf8 signaling following a loss of RA may stimulate the node to generate asymmetry in presomitic mesoderm, leading to left-right asymmetry in somitogenesis clock PMID: 17600781 FGF-8 is expressed at a high frequency in bone metastases of human prostate cancer and expression of FGF-8 in PC-3 prostate cancer cells increases their growth as intratibial tumors. PMID: 18386787 Decreased FGF8 signaling causes deficiency of GnRH in humans. PMID: 18596921 associated gene expression signature suggests potential mediators for FGF-8b actions on prostate cancer progression and metastasis PMID: 19415685

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.