Western blot: 1: 500 - 1: 1000. Immunohistochemistry on paraffin sections: 1: 50 - 1: 200. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
The C-X-C or alpha 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 (also designated 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 co-receptor for T-tropic HIV-1, and SDF-1 has been shown to inhibit HIV-1 infection. Six human SDF-1 isoforms exist due to alternative splicing of CXCL12, the gene encoding SDF-1. Three isoforms are known for mouse and rat. Alternate names: C-X-C motif chemokine 12, IRH, Intercrine reduced in hepatomas, PBSF, Pre-B cell growth- stimulating factor, SDF1A, SDF1B, Stromal cell-derived factor 1, hIRH