MOUSE ANTI HUMAN CD206

Manufacturer GENWAY
Category
Type Antibody
Specific against Human
Amount 0.1 mg
Host Mouse
ArtNr 20-783-314624
Available
Genway ID:
GWB-B2B449
Specificity:
CD206
Isotype:
IgG2a
Preparation:
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Buffer Solution:
Phosphate buffered saline pH7. 4
Preservative Stabilisers:
0. 09% Sodium Azide (NaN3)Approx. Protein Concentrations: IgG concentration 1. 0mg/ml
Immunogen:
Monocyte-derived dendritic cells.
Specificity:
Is specific for human CD206 otherwise known as macrophage mannose receptor (MMR) a transmembrane protein and member of the multilectin family of pattern recognition receptors (PRRs) which mediates phagocytosis and endocytosis and is modulated by a range of factors including cytokines immunoglobulin receptors and pathogens. CD206 has two extracellular lectin binding sites: the cysteine-rich domain binds to sulphated sugars of glycoproteins such as thyroid stimulating hormone whilst the recognition of mannose and fucose occurs through carbohydrate recognition domains (CRDs). The widespread distribution and recognition of a wide range of antigens by macrophages plays a key role in both innate and adaptive immunity with CD206 able to bind to both gram-negative and gram-positive bacteria mycobacterium yeasts fungi and parasites. The expression of CD206 is not restricted to macrophages but is also present on immature dendritic cells (DCs) endothelial cells kidney mesangial cells retinal pigment epithelium and tracheal smooth muscle cells. Recommended Secondary Antibodies: Rabbit Anti Mouse IgGGoat Anti Mouse IgGHuCAL Anti Mouse IgG2aRabbit Anti Mouse IgGGoat Anti Mouse IgG (H/L)Goat Anti Mouse IgG IgA IgMGoat Anti Mouse IgG (Fc)Sheep Anti Mouse IgG (H/L)
Function:
Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria fungi and other pathogens. Subcellular locationMembrane; Single-pass type I membrane protein.
Miscellaneous:
CRDs 1-3 have at most very weak affinity for carbohydrate. CRD 4 shows the highest affinity binding and has multispecificity for a variety of monosaccharides. At least 3 CRDs (4 5 and 7) are required for high affinity binding and endocytosis of multivalent glycoconjugates. Sequence similaritiesContains 8 C-type lectin domains. Contains 1 fibronectin type-II domain. Contains 1 ricin B-type lectin domain. 1. Akira S et al (2006) Pathogen recognition and innate immunity Cell; 124:783-8012. Iwasaki A et al (2004) Toll-like receptor control of the adaptive immune responses. Nat. Immunol. 5:987-95. 3. Yoneyama M et al (2004) The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5:730-7. Nat. Immunol. 5:730-737 [1] \" Complete sequencing and characterization of 21 243 full-length human cDNAs. \" Ota T. Suzuki Y. Nishikawa T. Otsuki T. Sugiyama T. Irie R. Wakamatsu A. Hayashi K. Sato H. Nagai K. Kimura K. Makita H. Sekine M. Obayashi M. Nishi T. Shibahara T. Tanaka T. Ishii S. Yamamoto J. Saito K. Kawai Y. Isono Y. Nakamura Y. Nagahari K. Murakami K. Yasuda T. Iwayanagi T. Wagatsuma M. Shiratori A. Sudo H. Hosoiri T. Kaku Y. Kodaira H. Kondo H. Sugawara M. Takahashi M. Kanda K. Yokoi T. Furuya T. Kikkawa E. Omura Y. Abe K. Kamihara K. Katsuta N. Sato K. Tanikawa M. Yamazaki M. Ninomiya K. Ishibashi T. Yamashita H. Murakawa K. Fujimori K. Tanai H. Kimata M. Watanabe M. Hiraoka S. Chiba Y. Ishida S. Ono Y. Takiguchi S. Watanabe S. Yosida M. Hotuta T. Kusano J. Kanehori K. Takahashi-Fujii A. Hara H. Tanase T. -O. Nomura Y. Togiya S. Komai F. Hara R. Takeuchi K. Arita M. Imose N. Musashino K. Yuuki H. Oshima A. Sasaki N. Aotsuka S. Yoshikawa Y. Matsunawa H. Ichihara T. Shiohata N. Sano S. Moriya S. Momiyama H. Satoh N. Takami S. Terashima Y. Suzuki O. Nakagawa S. Senoh A. Mizoguchi H. Goto Y. Shimizu F. Wakebe H. Hishigaki H. Watanabe T. Sugiyama A. Takemoto M. Kawakami B. Yamazaki M. Watanabe K. Kumagai A. Itakura S. Fukuzumi Y. Fujimori Y. Komiyama M. Tashiro H. Tanigami A. Fujiwara T. Ono T. Yamada K. Fujii Y. Ozaki K. Hirao M. Ohmori Y. Kawabata A. Hikiji T. Kobatake N. Inagaki H. Ikema Y. Okamoto S. Okitani R. Kawakami T. Noguchi S. Itoh T. Shigeta K. Senba T. Matsumura K. Nakajima Y. Mizuno T. Morinaga M. Sasaki M. Togashi T. Oyama M. Hata H. Watanabe M. Komatsu T. Mizushima-Sugano J. Satoh T. Shirai Y. Takahashi Y. Nakagawa K. Okumura K. Nagase T. Nomura N. Kikuchi H. Masuho Y. Yamashita R. Nakai K. Yada . Nakamura Y. Ohara O. Isogai T. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo. [2] \" The status quality and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \" The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon. [3] \" Shared and unique functions of the DExD/H-box helicases RIG-I MDA5 and LGP2 in antiviral innate immunity. \" Yoneyama M. Kikuchi M. Matsumoto K. Imaizumi T. Miyagishi M. Taira K. Foy E. Loo Y. -M. Gale M. Jr. Akira S. Yonehara S. Kato A. Fujita T. J. Immunol. 175:2851-2858(2005) [PubMed: 16116171] [Abstract]Cited for: FUNCTION. [4] \" Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. \" Saito T. Hirai R. Loo Y. -M. Owen D. Johnson C. L. Sinha S. C. Akira S. Fujita T. Gale M. Jr. Proc. Natl. Acad. Sci. U. S. A. 104:582-587(2007) [PubMed: 17190814] [Abstract]Cited for: FUNCTION INTERACTION WITH DDX58. [5] \" The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA. \" Li X. Ranjith-Kumar C. T. Brooks M. T. Dharmaiah S. Herr A. B. Kao C. Li P. J. Biol. Chem. 284:13881-13891(2009) [PubMed: 19278996] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2. 0 ANGSTROMS) OF 541-678 IN COMPLEX WITH RNA FUNCTION SUBUNIT MUTAGENESIS OF LYS-634 AND LYS-651 ZINC-BINDING SITES. [6] \" Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. \" Takahasi K. Kumeta H. Tsuduki N. Narita R. Shigemoto T. Hirai R. Yoneyama M. Horiuchi M. Ogura K. Fujita T. Inagaki F. J. Biol. Chem. 284:17465-17474(2009) [PubMed: 19380577] [Abstract]Cited for: STRUCTURE BY NMR OF 546-678 FUNCTION SUBCELLULAR LOCATION. [7] \" The regulatory domain of the RIG-I family ATPase LGP2 senses double-stranded RNA. \" Pippig D. A. Hellmuth J. C. Cui S. Kirchhofer A. Lammens K. Lammens A. Schmidt A. Rothenfusser S. Hopfner K. -P. Nucleic Acids Res. 37:2014-2025(2009) [PubMed: 19208642] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2. 6 ANGSTROMS) OF 537-678 FUNCTION SUBUNIT MUTAGENESIS OF LYS-634 ZINC-BINDING SITES.
Amount: 0.1 mg
Available: In stock
Listprice: €326.19
Discount: -10.0%
Price: €293.57
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