MIP-1 beta Recombinant Protein

20303

P14097

Murine

E. coli

7305459

Lyophilized

NP_038680.1

recombinants

Mus musculus

Recombinants or rec. proteins

chemokine (C-C motif) ligand 4

This product is for research use only.

APMGSDPPTS CCFSYTSRQL HRSFVMDYYE TSSLCSKPAV VFLTKRGRQI CANPSEPWVT EYMSDLELN

Act-2, Mip1b, Scya4, MIP-1B, AT744.1, C-C motif chemokine 4, Immune activation protein 2, ACT-2

Greater than 95% by SDS-PAGE gel and HPLC analyses.Endotoxin level is less than 0.1 ng per μg (1EU/μg).

Biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 20.0 - 100.0 ng/mL.

The lyophilized MIP-1 beta recombinant protein is stable for at least 2 years from date of receipt at -20˚C. Reconstituted MIP-1 beta is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚C. As with any protein, exposing MIP-1 beta recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

Both MIP-1 alpha and MIP-1 beta are structurally and functionally related CC chemokines. They participate in the host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells e.g. macrophages, lymphocytes and NK cells. While both MIP-1 alpha and MIP-1 beta exert similar effects on monocytes their effect on lymphocytes differ; with MIP-1 alpha selectively attracting CD8+ lymphocytes and MIP-1 beta selectively attracting CD4+ lymphocytes. Additionally, MIP-1 alpha and MIP-1 beta have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1 alpha and MIP-1 beta are active on human and murine hematopoietic cells. Recombinant murine MIP-1 beta is a 7.8 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.