Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. Sankala, M. et al. (2002) J. Biol. Chem. 277:33378. The ED50 for this effect is 0.5-2.5 µg/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse MARCO protein Gln70-Ser518, with an N-terminal 9-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | Marco |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 46.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 57-60 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
MARCO (macrophage receptor with collagenous structure), also known as SCARA2, is an 80 kDa type II transmembrane glycoprotein that belongs to the class A scavenger receptor family (1). Mouse MARCO consists of a 48 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 449 aa extracellular domain (ECD) that includes a stalk region, a collagen-like region, and one SRCR domain (2). Within the ECD, mouse MARCO shares 69% and 86% aa sequence identity with human and rat MARCO, respectively. It shares 18%-28% aa sequence identity with other mouse class A scavenger receptors CL-P1, SCARA3, SCARA5, and SR-A1/MSR. MARCO is constitutively expressed on the surface of splenic and lymph node macrophages (2, 3). Its expression is induced on Kupffer cells and alveolar macrophages by microbial infection, chemical irritants, and Th1 polarizing factors (3-5). MARCO binds LPS, lipoteichoic acid, and other determinants on Gram positive and Gram negative bacteria (2, 6-8). It also binds modified LDL, CpG oligonucleotides, UGRP1, silica, and TiO2 (2, 9-11). MARCO is required for the organization of the splenic marginal zone and the interaction of local macrophages and B cells (12, 13). The SRCR domain mediates binding of MARCO to its various ligands (3, 12), while the collagen-like region mediates assembly into a disulfide-linked trimeric molecule (2, 7). MARCO ligation induces, but is not required for the production of IL-12, NO, or TNF-alpha by macrophages (5, 6, 9). MARCO knockout mice show a reduced clearance of bacterial infections, reduced mast cell mediated silicosis, increased pulmonary inflammation, and increased sensitivity to ozone induced lung damage (4, 9, 14-16).
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