Biotinylated Myeloperoxidase Antibody

Description

Biotinylated Myeloperoxidase Antibody
Catalog number: B2010196
Lot number: Batch Dependent
Expiration Date: Batch dependent
Volume/Weight: 0.25 mg
pH: 7.4
Supplied as: Ready-to-use
Appearance: Solution
Applications: biotin-labelled antibodies specific to human Myeloperoxidase, a peroxidase enzyme mostly expressed in neutrophils, which produces hypohalous acids known for their antimicrobial activities. MPO is released in the blood when artery walls are damaged. Both monoclonal and polyclonal antibodies are available.
Storage: -20C
Keywords: Biotin Myeloperoxidase antibody, biotinylated Myeloperoxidase antibodies, biotin labelled Myeloperoxidase antibody, biotin-labelled Myeloperoxidase antibody
Grade: Biotechnology grade. All components are highly pure (minimum 99%). All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered on a 0.22 um.

References:
1: Aratani Y. Myeloperoxidase: Its role for host defense, inflammation, and
neutrophil function. Arch Biochem Biophys. 2018 Feb 15;640:47-52.

2: Ndrepepa G. Myeloperoxidase – A bridge linking inflammation and oxidative
stress with cardiovascular disease. Clin Chim Acta. 2019 Jun;493:36-51.

3: Antonelou M, Michaëlsson E, Evans RDR, Wang CJ, Henderson SR, Walker LSK,
Unwin RJ, Salama AD; RAVE-ITN Investigators. Therapeutic Myeloperoxidase
Inhibition Attenuates Neutrophil Activation, ANCA-Mediated Endothelial Damage,
and Crescentic GN. J Am Soc Nephrol. 2020 Feb;31(2):350-364.

4: Galijasevic S. The development of myeloperoxidase inhibitors. Bioorg Med Chem
Lett. 2019 Jan 1;29(1):1-7.

5: Chami B, Martin NJJ, Dennis JM, Witting PK. Myeloperoxidase in the inflamed
colon: A novel target for treating inflammatory bowel disease. Arch Biochem
Biophys. 2018 May 1;645:61-71.

6: Metzler KD, Fuchs TA, Nauseef WM, Reumaux D, Roesler J, Schulze I, Wahn V,
Papayannopoulos V, Zychlinsky A. Myeloperoxidase is required for neutrophil
extracellular trap formation: implications for innate immunity. Blood. 2011 Jan
20;117(3):953-9.

7: Mariani F, Roncucci L. Role of the Vanins-Myeloperoxidase Axis in Colorectal
Carcinogenesis. Int J Mol Sci. 2017 Apr 27;18(5):918.

8: Manchanda K, Kolarova H, Kerkenpaß C, Mollenhauer M, Vitecek J, Rudolph V,
Kubala L, Baldus S, Adam M, Klinke A. MPO (Myeloperoxidase) Reduces Endothelial
Glycocalyx Thickness Dependent on Its Cationic Charge. Arterioscler Thromb Vasc
Biol. 2018 Aug;38(8):1859-1867.

9: Huang J, Milton A, Arnold RD, Huang H, Smith F, Panizzi JR, Panizzi P.
Methods for measuring myeloperoxidase activity toward assessing inhibitor
efficacy in living systems. J Leukoc Biol. 2016 Apr;99(4):541-8.

10: Garai D, Pálinkás Z, Balla J, Kettle AJ, Nagy P. Measurements for Sulfide-
Mediated Inhibition of Myeloperoxidase Activity. Methods Mol Biol.
2019;2007:179-203.

11: Reiding KR, Franc V, Huitema MG, Brouwer E, Heeringa P, Heck AJR. Neutrophil
myeloperoxidase harbors distinct site-specific peculiarities in its
glycosylation. J Biol Chem. 2019 Dec 27;294(52):20233-20245.

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