CXCR-4 (V340) polyclonal antibody

The C-X-C or α chemokine family is characterized by a pair of cysteine residues separated by a single amino acid and primarily functions as chemoattractants for neutrophils. The C-X-C family includes IL-8, NAP-2, MSGA and stromal cell derived factor-1 or SDF-1. SDF-1 was originally described as a pre-B cell stimulatory factor, but has now been shown to function as a potent chemoattractant for T cells and monocytes but not neutrophils. Receptors for the C-X-C family are G protein coupled, seven pass transmembrane domain proteins which include IL-8RA, IL-8RB and fusin (variously referred to as LESTR or CXCR-4) . Fusin is highly homologous to the IL-8 receptors, sharing 37% sequence identity at the amino acid level. The IL-8 receptors bind to IL-8, NAP-2 and MSGA, while fusin binds to its cognate ligand, SDF-1. Fusin has been identified as the major coreceptor for T-tropic HIV-1 and SDF-1 has been shown to inhibit HIV-1 infection.

C-X-C chemokine receptor type 4; CXC-R4; CXCR-4; FB22; Fusin; HM89; LCR1; Leukocyte-derived seven; transmembrane domain receptor; LESTR; NPYRL; Stromal cell-derived factor 1 receptor; SDF-1 receptor; CD184; CXCR4

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of CXCR-4 (V340) polyclonal antibody at 1:500 dilution Lane1:Hela cell lysate Lane2:Raw264.7 cell lysate Lane3:H9C2 cell lysate