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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| CYK0088-10 | 7 days | 10 µg | $120.00 |
Select product before adding to cart
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| CYK0088-50 | 7 days | 50 µg | $290.00 | |||
| CYK0088-1 | 7 days | 1 mg | $2,160.00 |
Product Overview | |
| Name | BMP13 Human |
|---|---|
| Description | |
| Bone Morphogenetic protein-13 Human Recombinant | |
| Accession (Primary) | Q6KF10 |
| 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. | |
| Source | |
| Escherichia Coli. | |
| Physical Appearance | |
| Sterile Filtered White lyophilized (freeze-dried) powder. | |
| Formulation | |
| BMP-3 protein was lyophilized from a 0.2 µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. | |
| 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. | |
| 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 ED 50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells. | |
| Solubility | |
| It is recommended to reconstitute the lyophilized BMP3 in sterile 4mM HCl not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. | |
| 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. | |
| Precautions | |
| BMP13 Human is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( Q6KF10 ) | |
Background |
Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine Abstract: Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine. Introduction: Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts. Characteristics and Signaling Pathways: BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair. Production of BMP-13 Human Recombinant: Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein. Potential Therapeutic Applications: BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes. Conclusion: BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine. |
References |
Bibliography: Chubinskaya S, Segalite D, Pikovsky D, Hakimiyan A, Rueger DC. Effects induced by BMPS in cultures of human articular chondrocytes: comparative studies. Growth Factors. 2008;26(5):275-283. Lyons KM, Hogan BL, Robertson EJ. Colocalization of BMP 7 and BMP 2 RNAs suggests that these factors cooperatively mediate tissue interactions during murine development. Mech Dev. 1995;50(1):71-83. Vukicevic S, Luyten FP, Kleinman HK, Reddi AH. Differentiation of canalicular cell processes in bone cells by basement membrane matrix components: regulation by discrete domains of laminin. Cell. 1990;63(2):437-445. Zhu W, Rawlins BA, Boachie-Adjei O, et al. Combined bone morphogenetic protein-2 and -7 gene transfer enhances osteoblastic differentiation and spine fusion in a rodent model. J Bone Miner Res. 2004;19(12):2021-2032. Zhang W, Deng D, Lv D, et al. Role of bone morphogenetic protein 13 in osteogenic differentiation of rat dental follicle stem cells. Stem Cells Dev. 2012;21(11):library-1296. |
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