Viral MIP-II Antibody
R&D Systems, part of Bio-Techne | Catalog # AF601
Key Product Details
Species Reactivity
Validated:
Cited:
Applications
Validated:
Cited:
Label
Antibody Source
Product Specifications
Immunogen
Leu24-Arg94
Accession # NP_572064
Specificity
Clonality
Host
Isotype
Applications for Viral MIP-II Antibody
Western Blot
Sample: Recombinant Viral MIP-II (Catalog # 601-VB)
Formulation, Preparation, and Storage
Purification
Reconstitution
Formulation
Shipping
Stability & 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-II
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-II cDNA encodes a 94 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide that is cleaved to yield a 71 aa residue mature protein. Among human chemokines, vMIP-II is most closely related to MIP-1 alpha, sharing approximately 41% 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. vMIP-II binds to the CCR-3 chemokine receptor through which eotaxin and other beta chemokines activate eosinophils. vMIP-II has been shown to activate and chemoattract human eosinphils. 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.
References
- Moore, P.S. et al. (1996) Science 274:5293.
- Boshoff, C. et al. (1997) Science 278:290.
Long Name
Alternate Names
UniProt
Additional MIP-II Products
Product Documents for Viral MIP-II Antibody
Product Specific Notices for Viral MIP-II Antibody
For research use only