Recombinant Human Growth/Differentiation Factor 9 (GDF9) Protein (GST)

Name: Recombinant Human Growth/Differentiation Factor 9 (GDF9) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04390P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Growth/Differentiation Factor 9 (GDF9) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O60383
Target Symbol	GDF9
Synonyms	GDF9Growth/differentiation factor 9; GDF-9
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	GQETVSSELKKPLGPASFNLSEYFRQFLLPQNECELHDFRLSFSQLKWDNWIVAPHRYNPRYCKGDCPRAVGHRYGSPVHTMVQNIIYEKLDSSVPRPSCVPAKYSPLSVLTIEPDGSIAYKEYEDMIATKCTCR
Expression Range	320-454aa
Protein Length	Full Length of Mature Protein
Mol. Weight	42.5kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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	Required for ovarian folliculogenesis. Promotes primordial follicle development. Stimulates granulosa cell proliferation. Promotes cell transition from G0/G1 to S and G2/M phases, through an increase of CCND1 and CCNE1 expression, and RB1 phosphorylation. It regulates STAR expression and cAMP-dependent progesterone release in granulosa and thecal cells. Attenuates the suppressive effects of activin A on STAR expression and progesterone production by increasing the expression of inhibin B. It suppresses FST and FSTL3 production in granulosa-lutein cells.
Subcellular Location	Secreted.
Protein Families	TGF-beta family
Database References	HGNC: 4224 OMIM: 601918 KEGG: hsa:2661 STRING: 9606.ENSP00000296875 UniGene: PMID: 30039232 Data suggest that GDF9 and BMP15 are oocyte-secreted factors with leading roles in control of ovarian function in female reproduction, modulating both fate of somatic granulosa cells and quality/developmental competence of the egg. (GDF9 = growth and differentiation factor-9; BMP15 = bone morphogenetic protein-15) [REVIEW] PMID: 29544636 GDF9 single nucleotide polymorphism is not associated with Endometriosis-associated infertility. PMID: 28831646 GDF9 single nucleotide polymorphism is associated with fecundity. PMID: 28762037 Asiaticoside hindered the invasive growth of KFs by inhibiting the GDF-9/MAPK/Smad pathway. PMID: 28346732 Human GDF9 and BMP15 act synergistically to stimulate granulosa cell proliferation, a response that also involves species-specific non-SMAD signalling pathways. PMID: 25155366 these results indicated that the GDF9 C447T SNP is a possible candidate genetic risk factor for female infertility in the Polish population. PMID: 27035733 GDF-9 promotes the proliferation and migration of keloid fibroblasts via a mechanism involving the Smad2/3 pathway. PMID: 27855376 GDF9 c.169G>T (D57Y), c.546G>A (rs1049127), and BMP15 rs79377927 (788_789insTCT) were associated with premature ovarian failure in the Chinese Hui population. PMID: 25954833 results support a model of activation for human GDF9 dependent on cumulin formation through heterodimerization with BMP15. Oocyte-secreted cumulin is likely to be a central regulator of fertility in mono-ovular mammals. PMID: 26254468 GDF-9 and GDF-15 levels may influence bone parameters in polycystic ovary syndrome PMID: 24430093 GDF9 and BMP15 expression is reduced in primordial, primary, and secondary follicles in ovarian tissues of PCOS patients. PMID: 25172094 The arginine residue in the pre-helix loop of GDF9 homodimer may prevent the inhibition from its pro-domain or directly alter receptor binding, but this residue in GDF9 does not significantly affect the heterodimer activity. PMID: 25253739 Eleven unique copy number changes are identified in a total of 11 patients, including a tandem duplication of 475 bp, containing part of the GDF9 gene promoter region. PMID: 24939957 Data suggest up-regulation of mRNA for GDF9 and BMP15 (bone morphogenetic protein 15) in cumulus granulosa cells serves as biomarker for oocyte maturation, fertilization, embryo quality, and pregnancy in couples undergoing ICSI for male infertility. PMID: 25139161 These results suggest that COCs cultured with recombinant GDF9 in oocyte maturation medium improve oocyte developmental competence and subsequent developmental competence of cloned embryo in cattle. PMID: 24840335 Reduced expression of growth and differentiation factor-9 is associated with aggressive behaviour of clear-cell renal cell carcinoma. PMID: 25368253 Oocyte-derived GDF9 does not alter gap junction intercellular communication activity between human granulosa cells. PMID: 24413384 Alterations to hGDF9 synthesis and activity can contribute to the most common ovarian pathologies. PMID: 24438375 genetic association studies in population of Han women in China: Data suggest that a mutation in precursor region of GDF9 (R146C) is associated with premature ovarian failure (POF); R146C mutation found in 3 women with POF but absent in controls. PMID: 23851219 FOXL2 expression is required for GDF-9 stimulation of follistatin transcription. PMID: 23523567 BMP15 and GDF9 transcript levels increase in mature oocytes from women with polycystic ovary syndrome after ovarian stimulation, and might inhibit the progesterone secretion by follicular cells PMID: 22825968 findings that GDF9:BMP15 heterodimers are the most bioactive ligands in mice and humans compared with homodimers explain many puzzling genetic and physiological data and have important implications for improving female fertility in mammals PMID: 23382188 CDC6 and GDF-9 might be closely related to the carcinogenesis, clinical biological behaviors, and prognosis of gallbladder adenocarcinoma. PMID: 23011157 It was shown that human kidney tumours have a reduced or loss of expression of GDF9. In vitro, GDF9 overexpression suppresses the invasiveness, growth and migration of kidney cancer cells. PMID: 23060562 GDF-9 levels are inversely correlated with the growth, adhesion and migration of bladder cancer cells in vitro. PMID: 22159313 GDF9 may contribute to the variation observed in follicular development, ovulation rate, and fecundity between mammals PMID: 22234469 GDF9 decreases basal and activin A-induced FST and FSTL3 expression, and this explains, in part, its enhancing effects on activin A-induced inhibin beta(B)-subunit mRNA expression and inhibin B production in hGL cells PMID: 21829661 In the samples from girls/women, the number of developing follicles was greater with GDF9 or BMP15 alone than with no BMP15 or GDF9. PMID: 21632818 The expression of GDF9 and BMP15 in oocytes from patients with polycystic ovary syndrome cannot reach the normal level even after ovarian stimulation. PMID: 21669410 Higher mature GDF9 levels in the follicular fluid were significantly correlated with oocyte nuclear maturation and embryo quality. PMID: 21496799 GDF-9 signaling via ALK-5, can promote cell invasiveness PMID: 21116689 Integral role of GDF-9 and BMP-15 in ovarian function. PMID: 21226076 GDF-9 can promote the motile and adhesive capacity of PC-3 prostate cancer cells by up-regulating expression of FAK and paxillin in a Smad dependent manner, suggesting a pro-tumourigenic role for GDF-9 in prostate cancer. PMID: 21042764 Impaired production of BMP15 and GDF9 mature proteins derived from proproteins with mutation in the proregion. PMID: 20547206 Mutational analysis of the coding region of GDF9 among 216 Chinese polycystic ovary syndrome patients. Five novel missense mutations were discovered namely c.15C>G, c.118T>G, c.133A>G, c.1025A>T and c.1275C>A. PMID: 20705511 The detection of GDF9 and TGFbetaR1 at both at the protein and mRNA levels suggests that GDF9 may have functions in human preantral follicles. PMID: 20427239 GDF-9 c.G546A, but not c.G169A or c.C447T, is correlated with the poor ovarian stimulation and in vitro fertilization outcomes in women with diminished ovarian reserve. PMID: 20451184 GDF9 attenuates the suppressive effects of activin A on StAR expression and progesterone production by increasing the expression of inhibin B, which acts as an activin A competitor. PMID: 20660033 Cell growth was significantly increased in the GDF9 over-expressing cells compared to the two controls; apoptosis was decreased in the presence of GDF9. PMID: 20458753 GDF-9 concentration in women with severe endometriosis was lower than in those without PMID: 19931079 data demonstrate that polymorphisms in major folliculogenesis genes, GDF9, BMP15, AMH, and AMHR2, are not associated with polycystic ovary syndrome susceptibility. PMID: 20236105 Reduced GDF-9 expression in cumulus granulosa cells of patients with polycystic ovary syndrome (PCOS) appears to be associated with decreased long-term developmental potential of the oocytes of patients with PCOS. PMID: 19376510 Data show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. PMID: 20067794 2 synonymous mutations (c.447C>T, c.546G>A) & a novel missense variant (c.169G>T) were found in both premature ovarian failure patients & control subjects in the coding region of GDF9, indicating them as a novel polymorphism PMID: 19438907 Bone morphogenetic protein receptor type II is a receptor for growth differentiation factor-9 PMID: 12135884 interaction with bone morphogenetic protein-15 PMID: 12446716 BMP-15 and GDF-9 have roles in fertility; critical sequences are determined by mutagenesis PMID: 14970198 This case-control study revealed eight mutations in the GDF9 gene in women with premature ovarian failure PMID: 16278619 although mutations in BMP15 and GDF9 are not a major cause of ovarian insufficiency, they may be involved in premature ovarian failure PMID: 16645022

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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.

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