AnaSpec, a worldwide provider of custom and catalogue antibodies, has added hundreds of antibodies to its existing portfolio, including a number of interleukin and chemokine antibodies
Interleukin-32 (IL-32), whose expression is increased following activation by IL-2, was initially identified as a transcript (NK4) selectively expressed in lymphocytes and NK cells.
It was later re-isolated from an IL-18-treated lung carcinoma cell line and re-named IL-32.
IL-32 does not share sequence homology with known cytokine families and is highly expressed in immune tissues, existing in at least four differentially spliced isoforms.
Because treatment of human monocytic and mouse macrophage cells with IL-32 induces several proinflammatory cytokines such as TNF-, IL-8 and MIP-2, and because it is induced in human peripheral lymphocyte cells after mitogen stimulation and in epithelial cells by IFN-, it has been suggested that IL-32 may play a role in autoimmune and inflammatory diseases such as rheumatoid arthritis.
Rabbit anti-IL-32 polyclonal antibody was raised against a 15 amino acid peptide from near the C-terminus of human IL-32 (Genbank accession No AAH09401).
Anti-IL-32 reacts with IL-32 at the molecular weight of approximately 22-25 kDa on western blot.
Anti-IL-32 detects all isoforms of IL-32.
Chemokine antibodies.
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 have been identified as HIV coreceptors.
These coreceptors, as well as CD4, are needed to infect target cells.
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.
It is required for infection by the dual-tropic strains of HIV-1 and mediates CD-4 independent infection by HIV-2.
The -chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1.9,10 CXCR4 associates with the surface CD4-gp120 complex before HIV enters target cells.11 CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types.
Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells.
The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV binding sites.
Rabbit polyclonal CXCR4 antibody was raised against a peptide corresponding to amino acids near the amino terminus of human CXCR4.
