Recombinant Human Bone Morphogenetic Protein 15 (BMP15) Protein (His&Myc)

Name: Recombinant Human Bone Morphogenetic Protein 15 (BMP15) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01758P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Human Bone Morphogenetic Protein 15 (BMP15) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O95972
Target Symbol	BMP15
Synonyms	Growth/differentiation factor 9B
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	QADGISAEVTASSSKHSGPENNQCSLHPFQISFRQLGWDHWIIAPPFYTPNYCKGTCLRVLRDGLNSPNHAIIQNLINQLVDQSVPRPSCVPYKYVPISVLMIEANGSILYKEYEGMIAESCTCR
Expression Range	268-392aa
Protein Length	Full Length of Mature Protein
Mol. Weight	21.4 kDa
Research Area	Developmental Biology
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	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	HGNC: 1068 OMIM: 300247 KEGG: hsa:9210 STRING: 9606.ENSP00000252677 UniGene: Hs.532692
Associated Diseases	Ovarian dysgenesis 2 (ODG2); Premature ovarian failure 4 (POF4)

Gene Functions References

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
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
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
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
Mutations in BMP15 associated with primary ovarian insufficiency reduce mature protein production, activity, or synergy with GDF9. PMID: 28359091
Human GDF9 and BMP15 act synergistically to stimulate granulosa cell proliferation, a response that also involves species-specific non-SMAD signalling pathways. PMID: 25155366
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
BMP15 supplementation differentially modulates reductive metabolism and mitochondrial localization within the oocyte. PMID: 25721374
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
GDF9 and BMP15 expression is reduced in primordial, primary, and secondary follicles in ovarian tissues of PCOS patients. PMID: 25172094
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
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
BMP15 polymorphism is not associated with ovarian reserve. PMID: 25336710
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
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
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
BMP15 down-regulates StAR expression and decreases progesterone production in human granulosa cells, likely via ALK3-mediated SMAD1/5/8 signaling. PMID: 24140593
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
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
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
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
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
BMP15 uses preferentially BMPR1B as its type I receptor, suggesting an important role for the BMPR1B receptor in human female fertility PMID: 22294741
BMP15 is associated with high response to ovarian stimulation. PMID: 21565556
BMP15 gene mutations may be potentially associated with polycystic ovarian syndrome patients. PMID: 22014425
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
There were no statistically significant differences in embryo quality among the patients regarding follicular fluid BMP15 expression status. PMID: 21496799
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
Integral role of GDF-9 and BMP-15 in ovarian function. PMID: 21226076
Impaired production of BMP15 and GDF9 mature proteins derived from proproteins with mutation in the proregion. PMID: 20547206
Various missense variants of the BMP15 gene were identified among patients with premature ovarian failure. PMID: 20364024
data demonstrate that polymorphisms in major folliculogenesis genes, GDF9, BMP15, AMH, and AMHR2, are not associated with polycystic ovary syndrome susceptibility. PMID: 20236105
No significant difference was detected in the expression of BMP-15 between patients with polycystic ovary syndrome and controls. PMID: 19376510
Data show that show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. PMID: 20067794
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
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
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
Data show that bone morphogenetic protein-15 activates the Smad pathway in granulosa cell models. PMID: 12419820
interaction with growth and differentiation factor-9 and implication in aberrant ovarian phenotype PMID: 12446716
BMP-15 and GDF-9 have roles in fertility; critical sequences are determined by mutagenesis PMID: 14970198
Hypergonadotropic ovarian failure is associated with an inherited mutation of human bone morphogenetic protein-15 gene. PMID: 15136966
comparison of the molecular characteristics of BMP-15 of polyovulatory mice with that of monoovulatory humans PMID: 15809424
Missense mutations in the BMP15 gene are associated with ovarian failure PMID: 16508750
although mutations in BMP15 and GDF9 are not a major cause of ovarian insufficiency, they may be involved in premature ovarian failure PMID: 16645022
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
a BMP15 alteration,as a possible cause of ovarian failure, previously described as a mutation, is instead a polymorphism PMID: 17826728
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
phosphorylation state of rhBMP-15 and rhGDF-9 is a determinant of their agonistic and antagonistic activities PMID: 18006624
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

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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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