anti-CXCR4 antibody (Chemokine (C-X-C Motif) Receptor 4) (AA 328-338)

Details for Product anti-CXCR4 Antibody No. ABIN568905
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AA 328-338
(82), (19), (12), (12), (12), (12), (11), (9), (8), (6), (6), (6), (5), (4), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Human, Mouse (Murine), Rat (Rattus)
(260), (109), (57), (14), (3), (2), (1), (1), (1), (1), (1), (1)
(214), (44), (31), (15), (3)
This CXCR4 antibody is un-conjugated
(7), (5), (4), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
(215), (94), (68), (59), (58), (43), (29), (20), (10), (9), (8), (8), (7), (7), (4), (3), (2), (1), (1), (1), (1)
Pubmed 10 references available
Quantity 0.1 mg
Shipping to United States (Change)
Availability Discontinued
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Immunogen A peptide corresponding to amino acids 328-338 of human CXCR4
Specificity This antibody reacts to CXCR4 (CXC Chemokine Receptor 4). It will cross react with mouse and rat CXCR4.
Purification Protein G chromatography
Alternative Name CD184 / CXCR4 (CXCR4 Antibody Abstract)
Background 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: C-X-C chemokine receptor type 4, CXC-R4, CXCR-4, FB22, Fusin, HM89, LCR1, LESTR, Leukocyte-derived seven transmembrane domain receptor, NPYRL, SDF1 receptor, Stromal cell-derived factor 1 receptor
Gene ID 7852
NCBI Accession NP_001008540
UniProt P61073
Research Area CD Antigens, Surface Receptors of Immune Cells, Chemokines, Receptors
Restrictions For Research Use only
Format Liquid
Concentration 0,5 mg/mL
Buffer PBS. Filter sterilized. Sodium azide free.
Preservative Azide free
Handling Advice Avoid repeated freezing and thawing.
Storage -20 °C
Expiry Date 12 months
Background publications Dimitrov: "How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity." in: Cell, Vol. 91, Issue 6, pp. 721-30, 1998 (PubMed).

Lu, Berson, Chen et al.: "Evolution of HIV-1 coreceptor usage through interactions with distinct CCR5 and CXCR4 domains." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 12, pp. 6426-31, 1997 (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).

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).

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).

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).

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).

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).

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).

Loetscher, Geiser, OReilly et al.: "Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes." in: The Journal of biological chemistry, Vol. 269, Issue 1, pp. 232-7, 1994 (PubMed).

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