J774A.1 mouse reticulum cell sarcoma macrophage cell line was stained with Goat Anti-Mouse MMR/CD206 PE-conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2535P, filled histogram) or isotype control ...read more
Detects mouse MMR/CD206 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 45% cross-reactivity with recombinant human MMR is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
MRC1
Purity Statement
Antigen Affinity-purified
Innovator's Reward
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12 months from date of receipt, 2 to 8 °C as supplied.
Buffer
Supplied in a saline solution containing BSA and Sodium Azide.
Preservative
Sodium Azide
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for MMR/CD206/Mannose Receptor Antibody [Phycoerythrin]
CD206
CLEC13D
CLEC13Dmacrophage mannose receptor 1
C-type lectin domain family 13 member D
mannose receptor, C type 1
MMR
MMRCD206 antigen
MRC1
Background
The mouse Macrophage Mannose Receptor (MMR), also known as CD206 and MRC1 (mannose receptor C, type 1), is a 175 kDa scavenger receptor that is expressed on tissue macrophages, myeloid dendritic cells, and liver and lymphatic endothelial cells (1). It belongs to a family of receptors sharing similar protein structure that also includes DEC205, phospholipase A2 receptor, and Endo180 (2, 3). The mouse MMR protein is synthesized as a 1456 amino acid (aa) precursor that contains a 19 aa signal sequence, a 1369 aa extracellular region, a 21 aa transmembrane segment and a 47 aa cytoplasmic domain (4). Its extracellular region is composed of an N-terminal cysteine-rich domain, followed by a single fibronectin type II repeat, and eight C-type lectin carbohydrate recognition domains (CRD) (3‑5). Mouse to human, the extracellular region is 82% aa identical. The cysteine-rich domain mediates recognition of sulfated N-acetylgalactosamine, which occurs on some extracellular matrix proteins and is the terminal sugar of the unusual oligosaccharides present on pituitary hormones such as lutropin and thyrotropin (6). Several of the CRDs participate in the Ca2+-dependent recognition of carbohydrates showing a preference for branched sugars with terminal mannose, fucose or N‑acetylglucosamine (7). The cytoplasmic domain of MMR includes a tyrosine-based motif for internalization in clathrin-coated vesicles. Once internalized, ligands are released following acidification of phagosomes or endosomes, and the receptor recycles to the cell surface (3, 8). MMR mediates phagocytosis upon binding to target structures that occur on a variety of pathogenic microorganisms including Gram-negative and Gram-positive bacteria, yeasts, parasites, and mycobacteria. MMR also functions to maintain homeostasis through the endocytosis of potentially harmful glycoproteins associated with inflammation (2, 3).
East, L. and C. Isake (2002) Biochim. Biophys. Acta 1572:364.
Chieppa, M. et al. (2003) J. Immunol. 171:4552.
Figdor, C. et al. (2002) Nat. Rev. Immunol. 2:77.
Harris, N. et al. (1992) Blood 80:2363.
Taylor, M. et al. (1990) J. Biol. Chem. 265:12156.
Leteux, C. et al. (2000) J. Exp. Med. 191:1117.
Martinez-Pomares, L. et al. (2001) Immunobiology 204:527.
Feinberg, H. et al. (2000) J. Biol. Chem. 275:21539.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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