MMR/CD206/Mannose Receptor Antibody (685645) [Alexa Fluor® 488]

• Reactivity: Hu
• Applications: WB, IHC
• Clone: 685645
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Alexa Fluor 488

MMR/CD206/Mannose Receptor Antibody (685645) [Alexa Fluor® 488] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant human MMR/CD206
  Leu19-Lys1383 (Thr399Ala) & (Leu407Phe),
  Accession # P22897
• Specificity: Detects human MMR/CD206 in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant mouse (rm) MMR or recombinant human Mrc2 is observed. In Western blots, approximately 25% cross-reactivity with rmMMR is observed.
• Isotype: IgG2b
• Clonality: Monoclonal
• Host: Mouse
• Purity Statement: Protein A or G purified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry
  • Western Blot

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% 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 (685645) [Alexa Fluor® 488]

• 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 human Macrophage Mannose Receptor (MMR), also known as CD206 and MRC1 (mannose receptor C, type 1), is a 190 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 human MMR protein is synthesized as a 1456 amino acid (aa) precursor that contains an 18 aa signal sequence, a 1371 aa extracellular region, a 21 aa transmembrane segment and a 46 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, 4). Human and mouse MMR extracellular regions share 82% aa identity. 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 (5). 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 (6). 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 is recycled to the cell surface (3, 7). 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).

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.