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Chemokine (C-X-C Motif) Receptor 4 (CXCR4) antibody
Human, Mouse (Murine), Rat (Rattus)
Alternatives Western Blotting (WB)
|8 references available|
|Quantity||0.1 mg (0.5 mg/ml) (Variants)|
|Price||291.50 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 6 to 8 Business Days|
|Alternative name||CD184 / CXCR4|
|Immunogen||Peptide corresponding to amino acids 328-338 of human CXCR4|
|Cross-Reactivity||Human, Mouse (Murine), Rat (Rattus)|
|Description||Human immunodeficiency virus (HIV) and related viruses require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b and CCR8 in the chemokine receptor family, and four new human molecules GPR15, STRL33, GPR1 and V28 were recently identified as HIV coreceptors1. Among them, CXCR4 (fusin, LESTR or HUMSTR) is a principal coreceptor for T-cell tropic strains of HIV-1 fusion and entry of human white blood cells (2,3). CXCR4 is also required for the infection by dual-tropic strains of HIV-1 and mediates CD-4 independent infection by HIV-2 (4,5). The a-chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1 (6,7). CXCR4 associates with the surface CD4-gp120 complex before HIV enters target cells (8). CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types (2). Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells (2,5,10). The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV biding sites (10,11). Alternate Names: CXC-R4, CXCR-4, SDF-1 Receptor, Fusin, LESTR, LCR1, FB22, NPYRL, HM89, Leukocyte-Derived Seven Transmembrane Domain Receptor, Stromal Cell-Derived Factor 1 Receptor, C-X-C Chemokine Receptor type 4.|
|Synonyms||FB22, HM89, LAP3, LCR1, NPYR, WHIM, CD184, LESTR, NPY3R, NPYRL, HSY3RR, NPYY3R, D2S201E, Sdf1r, Cmkar4, PB-CKR, PBSF/SDF-1, MGC108696, CXCR4, MGC128682, cxcr4, cxcr4-B, CXC-R4-B, CXCR-4-B, MGC52882, MGC130802, fb22, hm89, lap3, lcr1, npyr, whim, cd184, lestr, npy3r, npyrl, CXC-R4, CXCR-4, hsy3rr, npyy3r, xcxcr4, d2s201e|
|Application Notes||Western blot: 1 - 2 ug/ml. Recommended Positive Control: HeLa. In HeLa, a 45 kDa band is observed. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.|
|Buffer||PBS with 0.05 % BSA and 0.05 % sodium azide|
|Storage||Store the antibody at 2 - 8 °C up to six months or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing. Shelf Life: one year from despatch.|
|Research Area||CD Antigens, Surface Receptors of Immune Cells, Chemokines, Receptors|
|Restrictions||For Research Use only|
|Western blot analysis of 15 ug of whole cell lysate from HeLa cells with anti-CXCR4 at 1 ug/ml.|
Feng, Broder, Kennedy et al.: "HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor." in: Science (New York, N.Y.), Vol. 272, Issue 5263, pp. 872-7, 1996 (PubMed).
Doranz, Rucker, Yi et al.: "A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors." in: Cell, Vol. 85, Issue 7, pp. 1149-58, 1996 (PubMed).
Berson, Long, Doranz et al.: "A seven-transmembrane domain receptor involved in fusion and entry of T-cell-tropic human immunodeficiency virus type 1 strains." in: Journal of virology, Vol. 70, Issue 9, pp. 6288-95, 1996 (PubMed).
Bleul, Farzan, Choe et al.: "The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry." in: Nature, Vol. 382, Issue 6594, pp. 829-33, 1997 (PubMed).
Oberlin, Amara, Bachelerie et al.: "The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1." in: Nature, Vol. 382, Issue 6594, pp. 833-5, 1997 (PubMed).
Lapham, Ouyang, Chandrasekhar et al.: "Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines." in: Science (New York, N.Y.), Vol. 274, Issue 5287, pp. 602-5, 1996 (PubMed).
Endres, Clapham, Marsh et al.: "CD4-independent infection by HIV-2 is mediated by fusin/CXCR4." in: Cell, Vol. 87, Issue 4, pp. 745-56, 1997 (PubMed).
Brelot, Heveker, Pleskoff et al.: "Role of the first and third extracellular domains of CXCR-4 in human immunodeficiency virus coreceptor activity." in: Journal of virology, Vol. 71, Issue 6, pp. 4744-51, 1997 (PubMed).