|Application ||WB, E|
|Calculated MW||83869 Da|
|Antigen Region||548-575 aa|
|Other Names||Myeloperoxidase, MPO, Myeloperoxidase, 89 kDa myeloperoxidase, 84 kDa myeloperoxidase, Myeloperoxidase light chain, Myeloperoxidase heavy chain, MPO|
|Target/Specificity||This MPO antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 548-575 amino acids from the C-terminal region of human MPO.|
|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||MPO Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
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Provided below are standard protocols that you may find useful for product applications.
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].
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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