Manufacturer GENWAY
Type Antibody
Specific against Mouse
Applications IP
Amount 0.1 mg
Host Rat
ArtNr 20-783-314604
Genway ID:
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
cultured LAK cells from Balb/c mice.
Recognises murine CD51 a 140 kD alpha subunit of the vitronectin receptor which is otherwise known as the intergrin alpha v chain. CD51 can form heterodimers at the cell surface with a variety of beta integrins including CD29 and CD61. Heterodimers of CD51/CD61 functions as a receptor for vitronectin and a wide array of RGD-containing proteins including fibronectin fibrinogen von Willebrand factor laminin thrombospondin and osteopontin. CD51/CD61 is primarily expressed on myeloid cells and activated T-cells. Alpha-V integrins may play a role in embryo implantation angiogenesis and wound healing. The RMV-7 antibody has been reported to block binding of CD51 to vitronectin fibronectin and CD31 in some cell types as well as blocking LAK cell cytotoxicity (1). Recommended Negative Controls: RAT IgG1 NEGATIVE CONTROLRecommended Secondary Antibodies: Goat Anti Rat IgGRabbit Anti Rat IgGGoat Anti Rat IgG (MOUSE ADSORBED)
The alpha-V integrins are receptors for vitronectin cytotactin fibronectin fibrinogen laminin matrix metalloproteinase-2 osteopontin osteomodulin prothrombin thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. Alpha-V integrins may play a role in embryo implantation angiogenesis and wound healing. Mice expressing a null mutation of the alpha-V subunit gene survive until late in embryonic development and occasionally even to birth. They demonstrate cleft palate and defective development of CNS and gastrointestinal blood vessels. Subunit structureInteracts with RAB25 By similarity. Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-V associates with either beta-1 beta-3 beta-5 beta-6 or beta-8. Subcellular locationMembrane; Single-pass type I membrane protein. Sequence similaritiesBelongs to the integrin alpha chain family. Contains 7 FG-GAP repeats. 1. Gardner L. et al. (2004) The human Duffy antigen binds selected inflammatory but not homeostatic chemokines. Biochem. Biophys. Res. Commun. 321:306-12. 2. Chaudhuri A. et al. (1993) Cloning of glycoprotein D cDNA which encodes the major subunit of the Duffy blood group system and the receptor for the Plasmodium vivax malaria parasite. PNAS 90:10793-7. 3. Gil M. L. et al (1992) A member of the tetra spans transmembrane protein superfamily is recognized by a monoclonal antibody raised against an HLA class I-deficient lymphokine-activated killer-susceptible B lymphocyte line. Cloning and functional studies. J. Immunol. ??? 2826-33. J. Immunol. 148(9):2826-33 [1] \" Cloning of glycoprotein D cDNA which encodes the major subunit of the Duffy blood group system and the receptor for the Plasmodium vivax malaria parasite. \" Chaudhuri A. Polyakova J. Zbrzezna V. Williams K. Gulati S. Pogo A. Proc. Natl. Acad. Sci. U. S. A. 90:10793-10797(1993) [PubMed: 8248172] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) PARTIAL PROTEIN SEQUENCE VARIANT ASP-42. Tissue: Bone marrow. [2] \" Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy-negative individuals. \" Tournamille C. Colin Y. Cartron J. -P. Le van Kim C. Nat. Genet. 10:224-228(1995) [PubMed: 7663520] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT ASP-42. Tissue: Blood. [3] \" Genomic organization of the glycoprotein D gene: Duffy blood group Fya/Fyb alloantigen system is associated with a polymorphism at the 44-amino acid residue. \" Iwamoto S. Omi T. Kajii E. Ikemoto S. Blood 85:622-626(1995) [PubMed: 7833467] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood. [4] \" Arg89Cys substitution results in very low membrane expression of the Duffy antigen/receptor for chemokines in Fy(x) individuals. \" Tournamille C. Le Van Kim C. Gane P. Le Pennec P. Y. Roubinet F. Babinet J. Cartron J. -P. Colin Y. Blood 92:2147-2156(1998) [PubMed: 9731074] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2) VARIANTS ASP-42; CYS-89 AND THR-100. Tissue: Blood. [5] \" The Fy(x) phenotype is associated with a missense mutation in the Fy(b) allele predicting Arg89Cys in the Duffy glycoprotein. \" Olsson M. L. Smythe J. S. Hansson C. Poole J. Mallinson G. Jones J. Avent N. D. Daniels G. Br. J. Haematol. 103:1184-1191(1998) [PubMed: 9886340] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS ASP-42; CYS-89 AND THR-100. [6] \" New polymorphisms in DARC. \" Doescher A. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT PHE-326. Tissue: Peripheral blood. [7] \" The DNA sequence and biological annotation of human chromosome 1. \" Gregory S. G. Barlow K. F. McLay K. E. Kaul R. Swarbreck D. Dunham A. Scott C. E. Howe K. L. Woodfine K. Spencer C. C. A. Jones M. C. Gillson C. Searle S. Zhou Y. Kokocinski F. McDonald L. Evans R. Phillips K. Atkinson A. Cooper R. Jones C. Hall R. E. Andrews T. D. Lloyd C. Ainscough R. Almeida J. P. Ambrose K. D. Anderson F. Andrew R. W. Ashwell R. I. S. Aubin K. Babbage A. K. Bagguley C. L. Bailey J. Beasley H. Bethel G. Bird C. P. Bray-Allen S. Brown J. Y. Brown A. J. Buckley D. Burton J. Bye J. Carder C. Chapman J. C. Clark S. Y. Clarke G. Clee C. Cobley V. Collier R. E. Corby N. Coville G. J. Davies J. Deadman R. Dunn M. Earthrowl M. Ellington A. G. Errington H. Frankish A. Frankland J. French L. Garner P. Garnett J. Gay L. Ghori M. R. J. Gibson R. Gilby L. M. Gillett W. Glithero R. J. Grafham D. V. Griffiths C. Griffiths-Jones S. Grocock R. Hammond S. Harrison E. S. I. Hart E. Haugen E. Heath P. D. Holmes S. Holt K. Howden P. J. Hunt A. R. Hunt S. E. Hunter G. Isherwood J. James R. Johnson C. J||?||hnson D. Joy A. Kay M. Kershaw J. K. Kibukawa M. Kimberley A. M. King A. Knights A. J. Lad H. Laird G. Lawlor S. Leongamornlert D. A. Lloyd D. M. Loveland J. Lovell J. Lush M. J. Lyne R. Martin S. Mashreghi-Mohammadi M. Matthews L. Matthews N. S. W. McLaren S. Milne S. Mistry S. Moore M. J. F. Nickerson T. O\' Dell C. N. Oliver K. Palmeiri A. Palmer S. A. Parker A. Patel D. Pearce A. V. Peck A. I. Pelan S. Phelps K. Phillimore B. J. Plumb R. Rajan J. Raymond C. Rouse G. Saenphimmachak C. Sehra H. K. Sheridan E. Shownkeen R. Sims S. Skuce C. D. Smith M. Steward C. Subramanian S. Sycamore N. Tracey A. Tromans A. Van Helmond Z. Wall M. Wallis J. M. White S. Whitehead S. L. Wilkinson J. E. Willey D. L. Williams H. Wilming L. Wray P. W. Wu Z. Coulson A. Vaudin M. Sulston J. E. Durbin R. M. Hubbard T. Wooster R. Dunham I. Carter N. P. McVean G. Ross M. T. Harrow J. Olson M. V. Beck S. Rogers J. Bentley D. R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. [8] \" 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] (ISOFORM 2) VARIANT PHE-326. Tissue: Lung. [9] \" Emergence of FY*A(null) in a Plasmodium vivax-endemic region of Papua New Guinea. \" Zimmerman P. A. Woolley I. Masinde G. L. Miller S. M. McNamara D. T. Hazlett F. Mgone C. S. Alpers M. P. Genton B. Boatin B. A. Kazura J. W. Proc. Natl. Acad. Sci. U. S. A. 96:13973-13977(1999) [PubMed: 10570183] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117 (ISOFORMS 1 AND 2). [10] \" Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites. \" Tournamille C. Filipe A. Wasniowska K. Gane P. Lisowska E. Cartron J. -P. Colin Y. Le Van Kim C. Br. J. Haematol. 122:1014-1023(2003) [PubMed: 12956774] [Abstract]Cited for: DISULFIDE BONDS GLYCOSYLATION AT ASN-16.
Amount: 0.1 mg
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