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Mip2 α

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MIP2-α is a recombinant mouse protein that functions as a chemokine. It plays a role in the inflammatory response by promoting the recruitment and activation of neutrophils. The core function of MIP2-α is to serve as a signaling molecule involved in cell migration and immune system processes.

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Lab products found in correlation

Kc gro, by Mesoscale (1 mentions) M csf, by Thermo Fisher Scientific (1 mentions) Rankl, by Thermo Fisher Scientific (1 mentions)

2 protocols using mip2 α

1

Quantifying Thrombus Protein Biomarkers

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Thrombus protein lysates were prepared by homogenization in T-PER Tissue Protein Extraction Reagent (Pierce) followed by centrifugation to remove cell debris according to the manufacturer’s instructions. The level in thrombus protein lysates of murine chemokine (C-X-C motif) ligand (CXCL)1 (KC), CXCL2 (MIP2-α) (R&D Systems), mouse PAI-2 total antigen (US Biologicals), and mouse PAI-1 total antigen (MPAIKT-TOT), total uPA (MUPAKT) and active uPA (MUPAKT-TOT)(Molecular Innovations) were analyzed by ELISA using commercial ELISA kits according to manufacturer’s instructions. Signals are expressed relative to total protein levels in the thrombus lysate, as determined by nanodrop or BioRad Protein assay, to normalize for any differences in clot size.
Siefert S.A., Chabasse C., Mukhopadhyay S., Hoofnagle M.H., Strickland D.K., Sarkar R, & Antalis T.M. (2014). Enhanced Venous Thrombus Resolution in Plasminogen Activator Inhibitor Type-2 Deficient Mice. Journal of thrombosis and haemostasis : JTH, 12(10), 1706-1716.
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2

In Vitro Osteoclast Generation

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For in vitro osteoclasts generation, bone marrow cells were obtained from wildtype BALB/c mice (Harlan), and CD-11b+ cells were cultured with M-CSF and RANKL (both Peprotech). Levels of CXCL1 (KC-GRO, Meso Scale Discovery) and CXCL2 (MIP-2α, R&D systems) were measured in the supernatants.
Wigerblad G., Bas D.B., Fernades-Cerqueira C., Krishnamurthy A., Nandakumar K.S., Rogoz K., Kato J., Sandor K., Su J., Jimenez–Andrade J.M., Finn A., Bersellini Farinotti A., Amara K., Lundberg K., Holmdahl R., Jakobsson P.J., Malmström V., Catrina A.I., Klareskog L, & Svensson C.I. (2015). Autoantibodies to citrullinated proteins induce joint pain independent of inflammation via a chemokine-dependent mechanism. Annals of the Rheumatic Diseases, 75(4), 730-738.
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