Recombinant Human BMP15 Protein

Beta LifeScience SKU/CAT #: BLA-0149P

Recombinant Human BMP15 Protein

Beta LifeScience SKU/CAT #: BLA-0149P
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Product Overview

Host Species Human
Accession O95972
Synonym BMP 15 BMP-15 BMP15 BMP15_HUMAN Bone morphogenetic protein 15 GDF 9B GDF-9B GDF9B Growth/differentiation factor 9B ODG2 POF4
Description Recombinant Human BMP15 Protein was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 29 kDa
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C.

Target Details

Target Function May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth.
Subcellular Location Secreted.
Protein Families TGF-beta family
Database References
Associated Diseases Ovarian dysgenesis 2 (ODG2); Premature ovarian failure 4 (POF4)

Gene Functions References

  1. The present mini-review provides an overview of recent findings relating GDF-9 and BMP-15 as fundamental factors implicated in the regulation of ovarian function and discusses their potential role as markers of oocyte quality in women. PMID: 30039232
  2. 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
  3. the expression of BMP15 in follicular fluid and Smad1 in granulosa cells was significantly decreased in the PCOS group compared with the control (P<0.05). The data suggested that the BMP15/Smad1 signalling pathway may be involved in granulosa cell apoptosis PMID: 28983616
  4. BMP15 did not seem critical for follicles to enter the growth phase. Genetic counselling should be performed and fertility preservation discussed before progressive loss of follicular reserve PMID: 28094433
  5. Mutations in BMP15 associated with primary ovarian insufficiency reduce mature protein production, activity, or synergy with GDF9. PMID: 28359091
  6. Human GDF9 and BMP15 act synergistically to stimulate granulosa cell proliferation, a response that also involves species-specific non-SMAD signalling pathways. PMID: 25155366
  7. 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
  8. BMP15 supplementation differentially modulates reductive metabolism and mitochondrial localization within the oocyte. PMID: 25721374
  9. 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
  10. GDF9 and BMP15 expression is reduced in primordial, primary, and secondary follicles in ovarian tissues of PCOS patients. PMID: 25172094
  11. The results showed no direct association between BMP15-9G or 852T and the development of premature ovarian failure (POF). Women with the 538A mutation are up to five times more likely to develop POF. The 788insTCT polymorphism had low biological impact. PMID: 25445105
  12. the BMP15 c.-9G allele is related to BMP15 increased transcription, supporting c.-9C>G as a causal agent of premature ovarian failure PMID: 25246117
  13. BMP15 polymorphism is not associated with ovarian reserve. PMID: 25336710
  14. BMP15 is a critical regulator of folliculogenesis and granulosa cell activities. Variations in BMP15 gene dosage have a relevant influence on ovarian function and can account for several defects of female fertility. PMID: 24980253
  15. Data suggest upregulation of mRNA for BMP15 and GDF9 (growth differentiation factor 9) in cumulus granulosa cells serves as biomarker for oocyte maturation, fertilization, embryo quality, and pregnancy in couples undergoing ICSI for male infertility. PMID: 25139161
  16. Oocyte-derived BMP15 decreases gap junction intercellular communication activity between human granulosa cells by down-regulating Cx43 expression, most likely via a Smad-dependent signaling pathway. PMID: 24413384
  17. BMP15 down-regulates StAR expression and decreases progesterone production in human granulosa cells, likely via ALK3-mediated SMAD1/5/8 signaling. PMID: 24140593
  18. Data from cultured mouse preantral follicles suggest that [human recombinant] BMP15 promotes follicle growth in short term (24 hours) incubation; subsequently BMP15 (48-72 hours) causes follicular atresia with increased granulosa cell apoptosis. PMID: 23782946
  19. genetic association studies in population of women in Spain: Data suggest an association between an SNP in BMP15 (rs3897937) and age at menopause; thus, duration of fertility in women may have genetic determinants involved in estrogen metabolism. PMID: 23173577
  20. 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
  21. the activation of bone morphogenetic protein 15 gene (BMP15) during the differentiation of human amniotic fluid stem cells (hAFSCs) into oocyte-like cells PMID: 22356426
  22. This study evaluated the levels of bone morphogenetic protein receptors BMPRIB and BMPRII mRNA in goat follicles and the effects of bone morphogenetic protein-15 (BMP-15) on the in vitro development of cultured preantral follicles. PMID: 22382392
  23. BMP15 uses preferentially BMPR1B as its type I receptor, suggesting an important role for the BMPR1B receptor in human female fertility PMID: 22294741
  24. BMP15 is associated with high response to ovarian stimulation. PMID: 21565556
  25. BMP15 gene mutations may be potentially associated with polycystic ovarian syndrome patients. PMID: 22014425
  26. 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
  27. 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
  28. There were no statistically significant differences in embryo quality among the patients regarding follicular fluid BMP15 expression status. PMID: 21496799
  29. Results describe a purified untagged human BMP15 mature region, which is stable and highly bioactive in human and rodent granulosa cells and as such is of importance for studies on human fertility. PMID: 20937357
  30. Integral role of GDF-9 and BMP-15 in ovarian function. PMID: 21226076
  31. Impaired production of BMP15 and GDF9 mature proteins derived from proproteins with mutation in the proregion. PMID: 20547206
  32. Various missense variants of the BMP15 gene were identified among patients with premature ovarian failure. PMID: 20364024
  33. data demonstrate that polymorphisms in major folliculogenesis genes, GDF9, BMP15, AMH, and AMHR2, are not associated with polycystic ovary syndrome susceptibility. PMID: 20236105
  34. No significant difference was detected in the expression of BMP-15 between patients with polycystic ovary syndrome and controls. PMID: 19376510
  35. Data show that show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. PMID: 20067794
  36. in Chinese premature ovarian failure patients, study revealed 3 variants in coding region of BMP15 - an insertion p.262insLeu in 5 patients & 2 novel mutations c.985C>T (p.Arg329Cys)& c.598C>T (p.His200Tyr) PMID: 19438907
  37. Results describe the expression and characterization of recombinant human BMP15, which is biologically active and very stable, and can induce the expression of a variety of mouse granulosa cell genes. PMID: 19651638
  38. Bone morphogenetic protein-15 is expressed in oocytes and cumulus granulosa cells and may play an important role in the hCG-induced oocyte final maturation and corpus luteum (CL) formation PMID: 19635612
  39. Data show that bone morphogenetic protein-15 activates the Smad pathway in granulosa cell models. PMID: 12419820
  40. interaction with growth and differentiation factor-9 and implication in aberrant ovarian phenotype PMID: 12446716
  41. BMP-15 and GDF-9 have roles in fertility; critical sequences are determined by mutagenesis PMID: 14970198
  42. Hypergonadotropic ovarian failure is associated with an inherited mutation of human bone morphogenetic protein-15 gene. PMID: 15136966
  43. comparison of the molecular characteristics of BMP-15 of polyovulatory mice with that of monoovulatory humans PMID: 15809424
  44. Missense mutations in the BMP15 gene are associated with ovarian failure PMID: 16508750
  45. although mutations in BMP15 and GDF9 are not a major cause of ovarian insufficiency, they may be involved in premature ovarian failure PMID: 16645022
  46. Mutational screening of the bone morphogenetic protein 15 (BMP15) and growth differentiation factor 9 (GDF9) genes in a population with premature ovarian failure (POF) identified no new mutations. PMID: 17027369
  47. a BMP15 alteration,as a possible cause of ovarian failure, previously described as a mutation, is instead a polymorphism PMID: 17826728
  48. We analyzed two polymorphisms (-9C>G and IVS1+905A>G) within the BMP15 gene in women from Spain with polycystic ovary syndrome (PCOS). BMP15 gene does not seem to be associated with PCOS. PMID: 17905236
  49. phosphorylation state of rhBMP-15 and rhGDF-9 is a determinant of their agonistic and antagonistic activities PMID: 18006624
  50. characterization of the post-translational modification of recombinant BMP-15 mature protein (P16 and P17); findings are the first knowledge of the structure of rhBMP-15 mature protein toward understanding the molecular basis of BMP-15 function PMID: 18227435

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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