Recombinant Rat MMR/CD206 Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Mannan is coated at 5 μg/mL (100 μL/well), the concentration of Recombinant Rat MMR/CD206 that produces 50% optimal binding response is 0.1-0.5 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived rat MMR/CD206 protein Leu26-Ala1395, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Starts at Leu26 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Mrc1 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
156.4 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. |
SDS-PAGE |
150-180 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat MMR/CD206 Protein, CF
Background
The MMR (macrophage mannose receptor) is also called MR due to its presence on cells other than macrophages, and is designated CD206, Mrc1 (mannose receptor C type 1), or CLEC13D (C-type lectin domain family 13, member D) (1‑4). CD206 is a 175 kDa endocytic receptor that is expressed on M2 alternatively activated tissue macrophages including tumor-associated macrophages (TAMs), inflammatory dendritic cells in selected lymphoid organs, and liver, splenic, lymphatic, and dermal microvascular endothelial cells (1, 2, 5‑8). The 1463 amino acid (aa) rat CD206 precursor contains a signal sequence (26 aa), an extracellular domain (ECD) containing an N‑terminal cysteine‑rich domain, a fibronectin type II (FNII) domain, eight C‑type lectin domains (CTLDs), and several N‑glycosylation sites (1369 aa), a transmembrane segment and a short (47 aa) cytoplasmic domain (2‑4). Metalloproteinases can mediate the shedding of the soluble ECD (2). The rat CD206 ECD shares 96% aa sequence identity with mouse CD206, and 84‑85% with human, equine, porcine and canine CD206. The cysteine‑rich domain recognizes some pituitary hormones such as LH (luteinizing hormone/lutropin) and TSH (thyroid stimulating hormone/thyrotropin), chondroitin sulfates, and sulfated N‑acetylgalactosamines including sulfo‑Lewis
a and ‑Lewis
x (1, 7, 9). The FNII domain mediates Ca2
+‑independent binding of collagens (2, 10). The CTLDs participate in Ca2
+‑dependent recognition of branched sugars with terminal mannose, fucose or N‑acetylglucosamine that occur on many pathogenic microorganisms (7, 11). CD206 internalizes ligands in clathrin‑coated vesicles, sorts them to phagosomes or early endosomes, and recycles to the cell surface (1, 6, 7). CD206 also promotes clearance of glycoproteins that promote allergy or ongoing inflammation, such as lysosomal hydrolases and myeloperoxidases (1, 2, 5‑7). It is involved in T cell polarization and production of pro‑ and anti‑inflammatory cytokines (1, 2). It facilitates peptide presentation on MHC II, and cross‑presentation on MHC I which is important for tumor immunogenicity (1, 2, 12). This function may be blocked by engagement of CD206 on TAMs by tumor mucins (8).
- Gazi, U. and L. Martinez-Pomares (2009) Immunobiology 214:554.
- Martinez-Pomares, L. (2012) J. Leukoc. Biol. 92:1177.
- Harris, N. et al. (1992) Blood 80:2363.
- Taylor, M.E. et al. (1990) J. Biol. Chem. 265:12156.
- Chieppa, M. et al. (2003) J. Immunol. 171:4552.
- Figdor, C. et al. (2002) Nat. Rev. Immunol. 2:77.
- Taylor, P.R. et al. (2005) Trends Immunol. 26:104.
- Allavena, P. et al. (2010) Clin. Dev. Immunol. 2010:547179.
- Leteux, C. et al. (2000) J. Exp. Med. 191:1117.
- Martinez-Pomares, L. et al. (2006) Eur. J. Immunol. 36:1074.
- Taylor, M.E. et al. (1992) J. Biol. Chem. 267:1719.
- Singh S.K. et al. (2011) Eur. J. Immunol. 41:916.
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