Recombinant Viral MIP-II Protein

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Summary
Reactivity VSpecies Glossary
Applications Bioactivity

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Recombinant Viral MIP-II Protein Summary

Details of Functionality
Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with mouse CCR3. The ED50 for this effect is 0.05-0.3 µg/mL.
Source
E. coli-derived viral MIP-II protein
Leu24-Arg94
Accession #
N-terminal Sequence
Leu24
Protein/Peptide Type
Recombinant Proteins
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
8.1 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
601-VB in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Viral MIP-II Protein

  • MIPII
  • MIP-II

Background

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.

  1. Moore, P.S. et al. (1996) Science 274:5293.
  2. Boshoff, C. et al. (1997) Science 278:290.

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Bioinformatics

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