MOUSE ANTI HUMAN DECTIN-1

DECTIN-1

Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant

Recognises human Dectin-1 also known as beta-glucan receptor (& #223; GR) a C-type lectin domain family member. It is a major pathogen pattern-recognition receptor that binds beta-glucans glucose polymers that form cell-wall components or exopolymers of yeasts fungi and some bacteria. Beta-glucans have also been used experimentally and therapeutically as immunomodulators that enhance resistance to bacterial yeast viral and protozoan infections as well as tumor formation. Dectin-1 also acts as a co-stimulatory molecule on T-cells to induce their proliferation and is necessary for the TLR2-mediated inflammatory response. It is highly expressed on peripheral blood leukocytes and dendritic cells. Human Dectin-1 has two major (& #223; GR-A and & #223; GR-B) and several minor isoforms. & #223; GR-A and & #223; GR-B differs by the presence and absence respectively of a stalk region. Clone BD6 recognises & #223; GR-A only. Recommended Negative Controls: MOUSE IgG2b NEGATIVE CONTROLRecommended Secondary Antibodies: Rabbit Anti Mouse IgGGoat Anti Mouse IgGRabbit Anti Mouse IgGGoat Anti Mouse IgGGoat Anti Mouse IgG (H/L)Goat Anti Mouse IgGGoat Anti Mouse IgG IgA IgMRabbit Anti Mouse IgGHuCAL Anti Mouse IgG2bGoat Anti Mouse IgG (Fc)Sheep Anti Mouse IgG (H/L) 1. Valenta T. et al. (2006) HIC1 attenuates Wnt signaling by recruitment of TCF-4 and Beta-catenin to the nuclear bodies. EMBO J. 25: 2326-2337. [1] \" Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation. \" Schaeper U. Boyd J. M. Verma S. Uhlmann E. Subramanian T. Chinnadurai G. Proc. Natl. Acad. Sci. U. S. A. 92:10467-10471(1995) [PubMed: 7479821] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 98-108 INTERACTION WITH E1A. Tissue: B-cell and Cervix carcinoma. [2] \" C-terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate polycomb proteins. \" Sewalt R. G. A. B. Gunster M. J. van der Vlag J. Satijn D. P. E. Otte A. P. Mol. Cell. Biol. 19:777-787(1999) [PubMed: 9858600] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] SEQUENCE REVISION FUNCTION. [3] \" Generation and annotation of the DNA sequences of human chromosomes 2 and 4. \" Hillier L. W. Graves T. A. Fulton R. S. Fulton L. A. Pepin K. H. Minx P. Wagner-McPherson C. Layman D. Wylie K. Sekhon M. Becker M. C. Fewell G. A. Delehaunty K. D. Miner T. L. Nash W. E. Kremitzki C. Oddy L. Du H. Sun H. Bradshaw-Cordum H. Ali J. Carter J. Cordes M. Harris A. Isak A. van Brunt A. Nguyen C. Du F. Courtney L. Kalicki J. Ozersky P. Abbott S. Armstrong J. Belter E. A. Caruso L. Cedroni M. Cotton M. Davidson T. Desai A. Elliott G. Erb T. Fronick C. Gaige T. Haakenson W. Haglund K. Holmes A. Harkins R. Kim K. Kruchowski S. S. Strong C. M. Grewal N. Goyea E. Hou S. Levy A. Martinka S. Mead K. McLellan M. D. Meyer R. Randall-Maher J. Tomlinson C. Dauphin-Kohlberg S. Kozlowicz-Reilly A. Shah N. Swearengen-Shahid S. Snider J. Strong J. T. Thompson J. Yoakum M. Leonard S. Pearman C. Trani L. Radionenko M. Waligorski J. E. Wang C. Rock S. M. Tin-Wollam A. -M. Maupin R. Latreille P. Wendl M. C. Yang S. -P. Pohl C. Wallis J. W. Spieth J. Bieri T. A. Berkowicz N. Nelson J. O. Osborne J. Ding L. Meyer R. Sabo A. Shotland Y. Sinha P. Wohldmann P. E. Cook L. L. Hickenbotham M. T. Eldred J. Williams D. Jones T. A. She X. Ciccarelli F. D. Izaurralde E. Taylor J. Schmutz J. Myers R. M. Cox D. R. Huang X. McPherson J. D. Mardis E. R. Clifton S. W. Warren W. C. Chinwalla A. T. Eddy S. R. Marra M. A. Ovcharenko I. Furey T. S. Miller W. Eichler E. E. Bork P. Suyama M. Torrents D. Waterston R. H. Wilson R. K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. [4] Mural R. J. Istrail S. Sutton G. G. Florea L. Halpern A. L. Mobarry C. M. Lippert R. Walenz B. Shatkay H. Dew I. Miller J. R. Flanigan M. J. Edwards N. J. Bolanos R. Fasulo D. Halldorsson B. V. Hannenhalli S. Turner R. Yooseph S. Lu F. Nusskern D. R. Shue B. C. Zheng X. H. Zhong F. Delcher A. L. Huson D. H. Kravitz S. A. Mouchard L. Reinert K. Remington K. A. Clark A. G. Waterman M. S. Eichler E. E. Adams M. D. Hunkapiller M. W. Myers E. W. Venter J. C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. [5] \" 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: Brain. [6] \" A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation tumorigenesis and metastasis. \" Boyd J. M. Subramanian T. Schaeper U. la Regina M. Bayley S. Chinnadurai G. EMBO J. 12:469-478(1993) [PubMed: 8440238] [Abstract]Cited for: INTERACTION WITH E1A PHOSPHORYLATION. [7] \" Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. \" Chakraborty S. Senyuk V. Sitailo S. Chi Y. Nucifora G. J. Biol. Chem. 276:44936-44943(2001) [PubMed: 11568182] [Abstract]Cited for: INTERACTION WITH MECOM. [8] \" Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C. \" Touitou R. Hickabottom M. Parker G. Crook T. Allday M. J. J. Virol. 75:7749-7755(2001) [PubMed: 11462050] [Abstract]Cited for: INTERACTION WITH EBV EBNA6. [9] \" Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. \" Vo N. Fjeld C. Goodman R. H. Mol. Cell. Biol. 21:6181-6188(2001) [PubMed: 11509661] [Abstract]Cited for: INTERACTION WITH NRIP1. [10] \" Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP). \" Hickabottom M. Parker G. A. Freemont P. Crook T. Allday M. J. J. Biol. Chem. 277:47197-47204(2002) [PubMed: 12372828] [Abstract]Cited for: INTERACTION WITH EBV EBNA3.