Viral MIP-I Antibody Summary
Ala25-Ala95
Accession # YP_001129366
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Chemotaxis Induced by MIP‑I and Neutralization by Viral MIP‑I Antibody. Recombinant Viral MIP-I (Catalog # 600-VA) chemoattracts the BaF3 mouse pro-B cell line transfected with human CCR8 in a dose-dependent manner (orange line). The amount of cells that migrated through to the lower chemotaxis chamber was measured by Resazurin (Catalog # AR002). Chemotaxis elicited by Recombinant Viral MIP-I (0.02 µg/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Viral MIP-I Monoclonal Antibody (Catalog # MAB799). The ND50 is typically 0.1-0.5 µg/mL.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: MIP-I
Human herpesvirus-8 (HHV‑8)/Kaposi’s sarcoma-associated herpesvirus (KSHV) is a gamma herpesvirus with homology to herpesvirus Saimiri and Epstein-Barr virus. HHV‑8 is etiologically linked to Kaposi’s sarcoma and a B-cell lymphoma known as primary effusion lymphoma. HHV‑8 has been shown to encode a variety of immunomodulatory proteins which were apparently pirated from cellular genes by the virus. Three chemokine-like proteins, vMIP-I, vMIP-II and vMIP-III have been found to be encoded within the HHV‑8 genome.
Viral MIP-I (also termed vMIP-1 alpha ) cDNA encodes a 95 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide that is cleaved to yield a 71 aa residue mature protein. Among human chemokines, vMIP-I is most closely related to MIP-1 alpha, sharing approximately 38% amino acid sequence identity. At the amino acid sequence level, vMIP-I and vMIP-II also share 48% identity. vMIP-I and vMIP-II are more closely related to one another phylogenetically than to other human chemokines, suggesting that they may have arisen by gene duplication within the virus rather than by two independent gene aquisitions. Both vMIP-I and vMIP-II have been shown to partially block HIV infection of peripheral blood mononuclear cells. vMIP-I and vMIP-II have also been found to be highly angiogenic in the chorioallantoic assay, suggesting that they may be partially responsible for the marked vascularity seen in KSHV-associated tumors.
Product Datasheets
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