- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-754
Synonyms
Bone morphogenetic protein 6, BMP-6, VG-1-related protein, VG-1-R, VGR-1, BMP6, VGR, VGR1.
Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules, which can induce ectopic bone growth. Various BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were initially identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based upon its expression early in embryogenesis, BMP6 has a suggested role in early development. Moreover, the fact that the BMP6 is closely related to BMP5 and BMP7 leads to an assumption of possible bone inductive activity.
Description
BMP6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (375-513) and having a molecular mass of 18kDa.
BMP6 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
BMP6 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile filtered colorless solution.
Formulation
The BMP6 solution (0.25mg/ml) contains 10mM Sodium citrate buffer (pH 3.5) and 10% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Safety Data Sheet
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSASSR RRQQSRNRST QSQDVARVSS ASDYNSSELK TACRKHELYV SFQDLGWQDW IIAPKGYAAN YCDGECSFPL NAHMNATNHA IVQTLVHLMN PEYVPKPCCA PTKLNAISVL YFDDNSNVIL KKYRNMVVRA CGCH.
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-6 Human Recombinant: Unraveling its Therapeutic Potential in Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-6 (BMP-6) human recombinant is a critical member of the bone morphogenetic protein family, known for its pivotal role in tissue development, repair, and regeneration. This research paper aims to provide a comprehensive analysis of BMP-6, including its characteristics, signaling pathways, and potential therapeutic applications. Moreover, innovative methodologies for the production and optimization of BMP-6 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 have emerged as promising approaches to address the challenges associated with tissue repair and regeneration. BMP-6, a prominent member of the BMP family, plays a key role in regulating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-6 and presents novel approaches for the production and optimization of BMP-6 human recombinant, aiming to unlock its therapeutic potential in diverse regenerative contexts.
Characteristics and Signaling Pathways:
BMP-6 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 pathways. BMP-6 signaling cascades, including Smad-dependent and Smad-independent pathways, orchestrate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.
Production of BMP-6 Human Recombinant:
Efficient production methodologies are vital for harnessing the therapeutic potential of BMP-6 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been employed for the production of functional BMP-6. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been implemented to enhance the yield and bioactivity of BMP-6 recombinant protein.
Potential Therapeutic Applications:
BMP-6 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its regulatory role in bone formation, cartilage regeneration, and wound healing positions it as a potential therapeutic candidate for the treatment of skeletal disorders, osteoarthritis, and tissue injuries. Furthermore, the ability of BMP-6 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in various regenerative processes.
Conclusion:
BMP-6 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 bone and cartilage formation, as well as wound healing, BMP-6 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
References
Bibliography:
- Balemans W, Van Hul W. Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev Biol. 2002;250(2):231-250.
- Celeste AJ, Iannazzi JA, Taylor RC, et al. Identification of transforming growth factor-beta family members present in bone-inductive protein purified from bovine bone. Proc Natl Acad Sci U S A. 1990;87(24):9843-9847.
- Heldin CH, Moustakas A. Signaling receptors for TGF-β family members. Cold Spring Harb Perspect Biol. 2016;8(8):a022053.
- Macías-Silva M, Hoodless PA, Tang SJ, et al. MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell. 1996;87(7):1215-1224.
- ten Dijke P, Yamashita H, Ichijo H, Franzen P, Laiho M, Miyazono K. Characterization of type I receptors for transforming growth factor-beta and activin. Science. 1994;264(5155):101-104.