protein

Recombinant Human Macrophage mannose receptor 1

MBS963867

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Macrophage mannose receptor 1

Macrophage mannose receptor 1

C-type lectin domain family 13 member D; C-type lectin domain family 13 member D-like; Macrophage mannose receptor 1-like protein 1; CD206

macrophage mannose receptor 1; Macrophage mannose receptor 1; macrophage mannose receptor 1; mannose receptor, C type 1; C-type lectin domain family 13 member D; C-type lectin domain family 13 member D-like; Human mannose receptor; hMR; Macrophage mannose receptor 1-like protein 1; CD_antigen: CD206

MRC1

MRC1; MRC1; MMR; hMR; CD206; MRC1L1; CLEC13D; CLEC13DL; bA541I19.1; CLEC13D; CLEC13DL; MRC1L1; MMR; hMR

MRC1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

655-1213

1456

RTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNK
EEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGS
PVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEH
LNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDY
QYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWK
YVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATG
EPNFANEDENCVTMYSNSGFW

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

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.

Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains.Taylor M.E., Conary J.T., Lennartz M.R., Stahl P.D., Drickamer K.J. Biol. Chem. 265:12156-12162(1990) Molecular characterization of the human macrophage mannose receptor demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.Ezekowitz R.A., Sastry K., Bailly P., Warner A.J. Exp. Med. 172:1785-1794(1990) Organization of the gene encoding the human macrophage mannose receptor (MRC1) .Kim S.J., Ruiz N., Bezouska K., Drickamer K.Genomics 14:721-727(1992) NHLBI resequencing and genotyping service (RS&G) The DNA sequence and comparative analysis of human chromosome 10.Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.Nature 429:375-381(2004) Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor.Taylor M.E., Bezouska K., Drickamer K.J. Biol. Chem. 267:1719-1726(1992) Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.Proteomics 8:3833-3847(2008) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor.Feinberg H., Park-Snyder S., Kolatkar A.R., Heise C.T., Taylor M.E., Weis W.I.J. Biol. Chem. 275:21539-21548(2000) Genetic and functional analysis of common MRC1 exon 7 polymorphisms in leprosy susceptibility.Alter A., de Leseleuc L., Van Thuc N., Thai V.H., Huong N.T., Ba N.N., Cardoso C.C., Grant A.V., Abel L., Moraes M.O., Alcais A., Schurr E.Hum. Genet. 127:337-348(2010)

4505245

NP_002429.1

NM_002438.3

P22897

80.33kD

Adaptive Immune System Pathway (1269171); Antigen Processing-Cross Presentation Pathway (1269195); Class I MHC Mediated Antigen Processing Presentation Pathway (1269192); Cross-presentation Of Soluble Exogenous Antigens (endosomes) Pathway (1269199); Immune System Pathway (1269170); Phagosome Pathway (153910); Phagosome Pathway (153859); Tuberculosis Pathway (213780); Tuberculosis Pathway (213743)

The recognition of complex carbohydrate structures on glycoproteins is an important part of several biological processes, including cell-cell recognition, serum glycoprotein turnover, and neutralization of pathogens. The protein encoded by this gene is a type I membrane receptor that mediates the endocytosis of glycoproteins by macrophages. The protein has been shown to bind high-mannose structures on the surface of potentially pathogenic viruses, bacteria, and fungi so that they can be neutralized by phagocytic engulfment.[provided by RefSeq, Sep 2015]

MRC1: 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. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Motility/polarity/chemotaxis; Receptor, misc.; Membrane protein, integral. Chromosomal Location of Human Ortholog: 10p12.33. Cellular Component: cell surface; endosome membrane; integral to plasma membrane; plasma membrane. Molecular Function: mannose binding; protein binding; receptor activity; transmembrane receptor activity; viral receptor activity. Biological Process: entry of virus into host cell; receptor-mediated endocytosis; signal transduction

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750