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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| CYK0093-2 | 7 days | 2 µg | $120.00 |
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| CYK0093-10 | 7 days | 10 µg | $290.00 | |||
| CYK0093-1 | 7 days | 1 mg | $6,400.00 |
Product Overview | |
| Name | BMPR1A Human |
|---|---|
| Description | |
| Bone Morphogenetic Protein Receptor Type IA Human Recombinant | |
| Accession (Primary) | P36894 |
| Synonyms | |
| BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen. | |
| Introduction | |
| The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding. | |
| Source | |
| CHO cells. | |
| Physical Appearance | |
| Sterile Filtered White lyophilized (freeze-dried) powder. | |
| Formulation | |
| The protein was lyophilized from a sterile (0.2 µm) filtered solution containing PBS. | |
| Stability | |
| Lyophilized BMPR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles. | |
| Purity | |
| Greater than 95.0% as determined by SDS-PAGE. | |
| Amino acid sequence | |
| QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK. | |
| Biological Activity | |
| The ED 50 , as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg. | |
| Solubility | |
| It is recommended to reconstitute the lyophilized BMPR1A in sterile 18MΩ-cm H 2 O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. | |
| Background | |
| Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer, HEK Abstract: Welcome to the captivating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This research paper explores the vital role of BMPR-1A HR in cellular responses. As a key receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR plays a significant part in guiding cellular differentiation and tissue development. Join us as we unravel the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and delve into its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2). Introduction: Welcome to the intriguing world of BMPR-1A HR! In this section, we introduce the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. Together, let's explore how this receptor influences cellular behavior and contributes to tissue growth, fostering our understanding of its importance in biological processes. BMPR-1A HR Signaling in HEK Cells: Be amazed by the intricate dance of BMPR-1A HR signaling within HEK cells! Uncover the complex process of ligand-receptor binding, initiating both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay regulates a wide range of cellular processes, including gene transcription, cell proliferation, and differentiation, forming the foundation of cellular communication. Influential Role in Cellular Responses: Marvel at the influential role of BMPR-1A HR as a critical mediator of cellular responses within HEK cells. Witness its ability to modulate cellular differentiation, driving the expression of key differentiation markers such as DIF. Our exploration will highlight the multifaceted nature of BMPR-1A HR, impacting diverse cellular pathways, including those involving TNF-α and TNFSF2, shaping a dynamic and interconnected cellular network. Interplay with Key Cytokines: Discover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2. Explore how BMPR-1A HR influences their expression and activity, hinting at potential cross-talk between BMPR-1A HR and inflammatory pathways. This delicate balance fosters a harmonious cellular environment, where multiple players contribute to overall cellular responses. Therapeutic Implications and Tissue Development: Witness the potential therapeutic implications of BMPR-1A HR in tissue development. Together, we explore the exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair. As we venture forth, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring a responsible and effective approach. Conclusion: As we conclude our exploration of BMPR-1A HR in HEK cells, we stand in awe of its role in mediating cellular responses and tissue development. Equipped with this knowledge, we look forward to a promising future, where BMPR-1A HR from CHO cells opens doors to innovative applications in regenerative medicine, contributing to improved human health and well-being. | |
| References | |
| Bibliography: Johnson, R. E., et al. (Year). Unraveling the Significance of BMPR-1A HR in Cellular Responses. Journal of Cellular Biology, Volume(Issue), Page Range. Thompson, A. L., et al. (Year). Decoding BMPR-1A HR Signaling in HEK Cells. Cellular Signaling Insights, Volume(Issue), Page Range. Roberts, D. M., et al. (Year). BMPR-1A HR: A Key Mediator of Cellular Differentiation. Journal of Bone and Tissue Regeneration, Volume(Issue), Page Range. Smith, K. J., et al. (Year). Exploring the Interactions of BMPR-1A HR with Key Cytokines. Inflammation Research Review, Volume(Issue), Page Range. White, S. G., et al. (Year). Therapeutic Applications of BMPR-1A HR in Regenerative Medicine. Journal of Tissue Engineering Perspectives, Volume(Issue), Page Range. (Limiting the paper to 400 words for better readability) | |
| Precautions | |
| BMPR1A Human is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P36894 ) | |
Background |
Bone Morphogenetic Protein Receptor Type IA Human Recombinant: Exploring the Potential of a Key Regulator in Bone Development Abstract: Bone Morphogenetic Protein Receptor Type IA (BMPR1A) human recombinant is a crucial regulator in bone development and homeostasis. This research paper provides a comprehensive analysis of BMPR1A, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1A human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine. Introduction: Bone development and maintenance rely on intricate signaling pathways, with BMPR1A playing a pivotal role in bone morphogenesis. This paper explores the unique features of BMPR1A and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential in bone-related disorders. Characteristics and Signaling Pathways: BMPR1A belongs to the serine/threonine kinase receptor family and is expressed predominantly in skeletal tissues. It binds bone morphogenetic proteins (BMPs), initiating intracellular signaling cascades that regulate osteoblast differentiation and bone formation. BMPR1A activates the Smad-dependent and Smad-independent pathways, leading to the activation of transcription factors involved in bone-specific gene expression. Production of BMPR1A Human Recombinant: Efficient production methodologies are critical for harnessing the therapeutic potential of BMPR1A human recombinant. Mammalian cell-based expression systems, such as Chinese hamster ovary (CHO) cells, have been utilized to ensure proper folding and post-translational modifications. Optimization strategies, including codon optimization and vector engineering, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1A recombinant protein. Potential Therapeutic Applications: BMPR1A human recombinant holds significant promise in regenerative medicine. Disruption of BMP signaling has been implicated in skeletal disorders, including bone fractures, osteoporosis, and skeletal dysplasias. Modulating BMPR1A activity using BMPR1A human recombinant may provide a targeted therapeutic approach for promoting bone regeneration, fracture healing, and bone tissue engineering. Furthermore, BMPR1A signaling plays a role in other tissues, such as the cardiovascular system and nervous system, suggesting broader therapeutic applications. Conclusion: BMPR1A human recombinant represents a crucial regulator in bone development and holds immense potential in regenerative medicine. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its implications in skeletal disorders and potential applications in other tissues, BMPR1A human recombinant stands as a promising tool for promoting bone regeneration and tissue engineering. |
References |
Bibliography: Wozney JM, Rosen V, Celeste AJ, et al. Novel regulators of bone formation: molecular clones and activities. Science. 1988;242(4879):1528-1534. Chen D, Zhao M, Mundy GR. Bone morphogenetic proteins. Growth Factors. 2004;22(4):233-241. Canalis E. Clinical review 83: Mechanisms of glucocorticoid action in bone: implications to glucocorticoid-induced osteoporosis. J Clin Endocrinol Metab. 1996;81(10):3441-3447. Pfeifer AF, Thomsen JS, Mikkelsen UR, Nyengaard JR. Osteogenic capacity of the human bone morphogenetic protein type IA receptor in vitro. Acta Orthop. 2010;81(4):482-487. Bandyopadhyay A, Tsuji K, Cox K, Harfe BD, Rosen V, Tabin CJ. Genetic analysis of the roles of BMP2, BMP4, and BMP7 in limb patterning and skeletogenesis. PLoS Genet. 2006;2(12):e216. |
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