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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| ABM0319-50 | 7 days | 50 µg | $600.00 |
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| ABM0319-100 | 7 days | 100 µg | $870.00 | |||
| ABM0319-150 | 7 days | 150 µg | $960.00 |
Product Overview | |
| Name | Heparanase 1 Clone HP3/17 |
|---|---|
| Description | |
| Heparanase 1 (HPA1), Monoclonal Anti-Human Antibody | |
| Synonyms | |
| Heparin, Porcine Heparin, Heparin Pig. | |
| Source | |
| Porcine Mucosa. | |
| Physical Appearance | |
| Sterile Filtered White lyophilized (freeze-dried) powder. | |
| Formulation | |
| The protein (1mg/ml) was lyophilized with no additives. | |
| Stability | |
| Lyophilized Heparin Sodium Porcine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heparin Sodium Porcine 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. | |
| Biological Activity | |
| 200IU/mg. | |
| Solubility | |
| It is recommended to reconstitute the lyophilized Heparin Sodium Porcine in sterile 18MΩ-cm H 2 O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. | |
| Background | |
| Heparin sodium, a highly sulfated glycosaminoglycan, has long been recognized for its pivotal role as an anticoagulant. In porcine systems, the study of Heparin Sodium takes on significance not only for its therapeutic applications in veterinary medicine but also for its potential translational impact on human health. This research embarks on an exploration of Heparin Sodium in porcine contexts, unraveling its structural intricacies, pharmacological attributes, and broader implications for health and biomedical interventions. By delving into the properties of Heparin Sodium in porcine models, scientists aim to deepen our understanding of its anticoagulant mechanisms, therapeutic potential, and the potential avenues for cross-species applications in healthcare. Structural Insights into Porcine Heparin Sodium: Porcine-derived Heparin Sodium, similar to its counterparts in other species, possesses a complex and highly sulfated structure. Understanding the nuances of its structure is fundamental for deciphering how Heparin Sodium interacts with antithrombin, leading to the inhibition of clotting factors and preventing the formation of blood clots. Structural insights contribute to optimizing its therapeutic efficacy. Pharmacological Attributes and Anticoagulant Mechanisms: Heparin Sodium's pharmacological attributes are central to its anticoagulant effects. In porcine systems, Heparin Sodium acts as an indirect anticoagulant by accelerating the activity of antithrombin, a natural inhibitor of clotting factors. Elucidating the specific mechanisms by which porcine Heparin Sodium modulates coagulation pathways contributes to refining its dosage and application in veterinary medicine. Therapeutic Potential in Veterinary Medicine: Porcine Heparin Sodium holds significant therapeutic potential in veterinary medicine, where clotting disorders and thrombotic events are prevalent. Understanding its pharmacokinetics, dosage requirements, and potential interactions with other drugs is crucial for optimizing its use in porcine healthcare. Additionally, exploring its safety profile in porcine models contributes to ensuring the well-being of animals under treatment. Cross-Species Applications and Translational Insights: Beyond its veterinary applications, porcine Heparin Sodium provides insights into potential cross-species applications, particularly in translational medicine. Understanding the similarities and differences in its anticoagulant mechanisms between porcine and human systems may open avenues for therapeutic innovations with relevance to both animal and human health. Challenges and Future Directions: While porcine Heparin Sodium presents opportunities for advancements in veterinary medicine and translational research, challenges persist. Fine-tuning its applications, addressing potential variations in its anticoagulant properties across different porcine breeds, and ensuring its safety and efficacy in diverse clinical scenarios are critical considerations for translational success. Porcine Heparin Sodium emerges as a key player in the landscape of anticoagulation, offering a bridge between veterinary and translational medicine. Its structural insights, pharmacological attributes, and therapeutic potential in porcine systems contribute not only to veterinary care but also offer translational insights with implications for human health. As researchers continue to unravel the molecular intricacies of porcine Heparin Sodium, they not only deepen our understanding of anticoagulation in veterinary contexts but also pave the way for innovative biomedical applications, shaping the future of healthcare for both animals and humans. | |
| Precautions | |
| Heparanase 1 Clone HP3/17 is for research use only and not for use in diagnostic or therapeutic procedures. | |
References |
1. I. Vlodavsky, Y. Friedmann, M. Elkin, H. Aingorn, R. Atzmon, R. Ishai-Michaeli, M. Bitan, O. Pappo, T. Peretz, I. Michal, L. Spector, I. Pecker. 1999. Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. Nat. Med. 5: 793–802. 2. I. Vlodavsky, Y. Friedman. 2001. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J. Clin. Invest. 108: 341–347. 3. C.R. Parish, C. Freeman, M.D. Hulett. 2001. Heparanase: a key enzyme involved in cell invasion. Biochem. Biophys. Acta 1471: M99–M108. 4. I. Vlodasvsky, G. Korner, R. Ishai-Michaeli, P. Bashkin, R. Bar-Shavit, Z. Fuks, 1990. Extracellular matrix-resident growth factors and enzyme: Possible involvement in tumor metastasis and angiogenesis. Cancer Metastasis Rev. 9: 203-226. 5. P. Bashkin, S. Doctrow, M. Klagsbrun, C.M. Svahn, J. Folkman, I. Vlodavsky. 1989. Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and hprn-like molecules. Biochemistry 28: 1737-1743. 6. M.B. Fairbanks, A.M. Mildner, J.W. Leone, G.S. Cavey, W.R. Mathews, R.F. Drong, J.L. Slightom, M.J. Bienkowski, C.W. Smith, C.A. Bannow, R.L. Heinrikson. 1999. Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer. J. Biol. Chem. 274: 29587– 29590. 7. A. Koliopanos, H. Friess, J. Klee., X. Shi, Q. Liao, I. Pecker, I. Vlodavsky, A. Zimmermann, M.W. Buchler. 1992. Heparanase expression in primary and metastatic pancreatic cancer. Cancer Res. 61: 4655–4659. 8. K. Gohji, H. Hirano, M. Okamoto, S. Kitazawa, M. Toyoshima, J. Dong, Y. Katsuoka, M. Nakajima. 2001. Expression of three extracellular matrix degradative enzymes in bladder cancer. Int. J. Cancer 95: 295–301. |
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