- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-937
Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
Description
BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.
The BMP-3 is purified by proprietary chromatographic techniques.
The BMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Solubility
It is recommended to reconstitute the lyophilized BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
Biological Activity
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
References
Bibliography:
- Groppe JC, Shore EM, Kaplan FS. BMP-3 Mutations in Humans Cause a Range of Phenotypes that Mimic Bone Morphogenetic Protein Receptor Disorders. Am J Hum Genet. 2002;70(3):709-717.
- Nishimura R, Wakabayashi M, Hata K, Matsubara T, Honma S, Wakisaka S. Immunohistochemical localization of bone morphogenetic protein-3 (osteogenin) in human and rat tissues. J Histochem Cytochem. 1994;42(6):731-742.
- Rosen V. BMP and BMP inhibitors in bone. Ann N Y Acad Sci. 2006;1068:19-25.
- Celeste AJ, Iannazzi JA, Taylor RC, et al. Identification of transforming growth factor β family members present in bone-inductive protein purified from bovine bone. Proc Natl Acad Sci U S A. 1990;87(24):9843-9847.
- Wozney JM, Rosen V, Celeste AJ, et al. Novel regulators of bone formation: molecular clones and activities. Science. 1988;242(4879):1528-1534.