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

Beta LifeScience SKU/CAT #: BLC-00168P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

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

Beta LifeScience SKU/CAT #: BLC-00168P
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Product Overview

Description Recombinant Sheep 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.
Activity Not tested.
Uniprotkb Q9MZE2
Target Symbol BMP15
Synonyms (BMP-15)(Growth/differentiation factor 9B)(GDF-9B)
Species Ovis aries (Sheep)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence QAGSIASEVPGPSREHDGPESNQCSLHPFQVSFQQLGWDHWIIAPHLYTPNYCKGVCPRVLHYGLNSPNHAIIQNLVSELVDQNVPQPSCVPYKYVPISILLIEANGSILYKEYEGMIAQSCTCR
Expression Range 269-393aa
Protein Length Full Length of Mature Protein
Mol. Weight 21.3 kDa
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 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

Gene Functions References

  1. activin can explain that the effects of BMP15 mutations differ when present in different genetic backgrounds PMID: 28069901
  2. BMP15 mutation is associated with prolificacy and female sterility. PMID: 28506298
  3. Studied polymorphism of BMP15 gene exon 1 using single strand conformational polymorphism (SSCP) and direct DNA sequencing methods in 170 Mehraban and Lori sheep ewes. PMID: 27565869
  4. study concluded that growth differentiation factor 9 and bone morphogenetic protein 15 follow stage-specific pattern of expression during the in vivo development of ovarian follicles in sheep, and in vitro culture altered these changes PMID: 26474685
  5. two novel mutations in the BMP15 gene are associated with increased litter size and ovulation rate PMID: 23637641
  6. Combined effect analyses indicated an extremely significant interaction between the random combinations of BMPR-IB, BMP-15 and FSHR genes on litter size. PMID: 25993301
  7. A higher number of oocytes proven to be competent for in vitro development and embryo survival after transfer are recovered from R+ ewes, despite the lower mean size of their follicles at puncture. PMID: 23438026
  8. The Lleyn breed was the most likely source of the BMP15 FecX(G) and GDF9 FecG(H) mutations in Belclare and Cambridge sheep, and the BMP15 FecX(B) mutation came from the High Fertility line developed from prolific ewes in commercial flocks in Ireland. PMID: 23301039
  9. Studies indicate that in BMP15-Knockout sheep, oocytes die as follicles start to grow. PMID: 23417416
  10. DNA polymorphism studies of BMP 15 gene in Corriedale and local Kashmir valley sheep (Ovis aries). PMID: 22425967
  11. A mutation in the bone morphogenetic protein 15 gene (FecXR allele) causes increased prolificity in heterozygous and sterility in homozygous ewes. PMID: 21622876
  12. It is concluded that the mutation in the BMP15 gene in I+ ewes leads to an earlier acquisition of LH responsiveness by granulosa cells in a greater proportion of follicles and this accounts for the small higher ovulation-rate in these animals. PMID: 19535491
  13. Data suggest an interaction between BMP15 levels and nutritional signals in the follicle to control ovulation rate; studies involved heterozygous Inverdale ewes. PMID: 21871206
  14. investigation of regulation of gene expression of BMP15 in ovulation: Higher ovulation rate in BB sheep (homozygous for mutation in BMPR1B) is due, at least in part, to low oocyte-derived BMP15 mRNA levels. PMID: 21474605
  15. 11-point mutations of BMP1B, BMP15, and GDF9 genes of 97 Bonpala ewes were genotyped. PMID: 21774623
  16. A significant association was found between BMP15 gene HinfI polymorphism and litter size in fat-tailed sheep. The heterozygous genotype showed higher litter size. PMID: 21327517
  17. These heterozygous genotypes resulted in higher ovulation rates, illustrating that one copy of each of the BMP15 and GDF9 mutations had equivalent effects on the ovulation rate. PMID: 19144040
  18. BMP15 has an essential role in ovarian folliculogenesis and the control of ovulation rate in sheep. PMID: 17038554
  19. Small Tailed Han ewes carrying mutations in both BMPR-IB and BMP-15 genes had greater litter size than those with either mutation alone. PMID: 17040942
  20. sequence of the complete coding region of BMP15 gene and determination of the patterns of expression of mRNAs encoding BMP15 PMID: 17715428
  21. in BMP15, this new mutation is associated with increased prolificacy and sterility in heterozygous and homozygous ewes respectively PMID: 18355397
  22. Expression patterns of 4 maternal effect genes (ZAR1, MATER, GDF9, and BMP15) were determined in ovine oocytes and in vitro-produced preimplantation embryos [ZAR1]. PMID: 19007555

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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