Myeloperoxidase Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
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Primary Accession | P05164 |
Other Accession | NP_000241.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 83869 Da |
Antigen Region | 60-89 aa |
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 |
Target/Specificity | This Myeloperoxidase antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 60-89 amino acids from the N-terminal region of human Myeloperoxidase. |
Dilution | WB~~1:1000 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Myeloperoxidase Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | MPO (HGNC:7218) |
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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 during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of netrophils. [provided by 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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