Mouse MARCO HEK293 Overexpression Lysate: Product Information
This Mouse MARCO overexpression lysate was created in HEK293 Cells and intented for use as a Western blot (WB) positive control. Purification of MARCO protein (Cat: 50283-M07H) from the overexpression lysate was verified.
A DNA sequence encoding the extracellular domain of mouse MARCO (NP_034896.1) (Gln 70-Ser 518) was expressed, fused with a polyhistidine tag at the N-terminus.
The secreted recombinant mouse MARCO consists of 465 amino acids and has a calculated molecular mass of 47.3 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 55-60 kDa band in SDS-PAGE under reducing conditions.
Mouse MARCO HEK293 Overexpression Lysate: Usage Guide
Cell lysate was prepared by homogenization of the over-expressed cells in ice-cold modified RIPA Lysis Buffer with cocktail of protease inhibitors (Sigma). Cell debris was removed by centrifugation. Protein concentration was determined by Bradford assay (Bio-Rad protein assay, Microplate Standard assay). The cell lysate was boiled for 5 min in 1 x SDS loading buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% b-mercaptoethanol, and lyophilized.
Macrophage receptor MARCO, also known as Macrophage receptor with collagenous structure and Marco, is a single-pass type II membrane protein. MARCO is a member of the class A scavenger receptor family and is part of the innate antimicrobial immune system. It is expressed in subpopulations of macrophages in the spleen and the medullary cord of lymph nodes. Although it is expressed on subsets of macrophages, it can be upregulated on other macrophages after bacterial infection. The strategic position of MARCO-expressing cells in lymphoid organs suggests an important role for this bacteria-binding molecule in removal of pathogens. MARCO has a short N-terminal cytoplasmic domain, a transmembrane domain, and a large extracellular part composed of a 75-residue long spacer domain, a 27-residue collagenous domain, and a 99-residue long scavenger receptor cysteine-rich (SRCR) domain. It is possible that cooperation between the SRCR domain and the collagenous domain is needed for high-affinity bacterial binding, or that the SRCR domain has to be in a trimeric form to effectively bind to bacteria
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