MPO Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P05164 |
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Clone Names | 101229017 |
Gene ID | 4353 |
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Other Names | Myeloperoxidase, MPO, Myeloperoxidase, 89 kDa myeloperoxidase, 84 kDa myeloperoxidase, Myeloperoxidase light chain, Myeloperoxidase heavy chain, MPO |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | MPO |
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Function | Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity (PubMed:9922160). Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (PubMed:25698971). |
Cellular Location | Lysosome. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Myeloperoxidase (MPO) is a heme protein synthesized duringmyeloid differentiation that constitutes the major component ofneutrophil azurophilic granules. Produced as a single chainprecursor, myeloperoxidase is subsequently cleaved into a light andheavy chain. The mature myeloperoxidase is a tetramer composed of2 light chains and 2 heavy chains. This enzyme produces hypohalousacids central to the microbicidal activity of netrophils. [providedby RefSeq].
References
Banerjee, M., et al. Toxicol. Appl. Pharmacol. 249(1):47-54(2010)Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)Nahon, P., et al. Antioxid. Redox Signal. (2010) In press :Wang, Y., et al. J. Huazhong Univ. Sci. Technol. Med. Sci. 30(4):437-442(2010)Hua, F., et al. Zhongguo Fei Ai Za Zhi 13(2):122-127(2010)
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