| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 14.3 kDa, a single non-glycosylated polypeptide chain containing 130 amino acids, with Avi tag at the C-terminus. |
| AA Sequence: |
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFAGLNDI FEAQKIEWHE |
| Purity: |
> 97% by SDS-PAGE and HPLC analyses. |
| Biological Activity: |
Fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.0, 5% Trehalose, 0.02% Tween-20. |
| Endotoxin: |
Less than 1 EU/μg of rHuMIF, Avi as determined by LAL method. |
| Reconstitution: |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
| Stability & 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. |
| Background: |
Migration inhibitory factor (MIF) is a secreted protein without a cleavable signal sequence and is released via a specialized, nonclassical pathway. It is secreted by macrophages in response to bacterial lipopolysaccharide (LPS) or M. tuberculosis antigens. MIF is composed of two α-helices and six β-strands, with four β-strands forming a β-sheet and the remaining two interacting with other MIF molecules to form a trimer. Structure-function studies suggest that MIF is bifunctional with distinct regions for different activities. The N- and C-termini are theorized to mediate enzymatic activity, specifically phenylpyruvate tautomerase activity, which depends on the Pro at position 1. Additionally, amino acids 50-65 are believed to have thiol-protein oxidoreductase activity. MIF exhibits proinflammatory cytokine activity, particularly in the region of amino acids 49-65. On fibroblasts, MIF induces the expression of IL-1, IL-8, and MMP, while on macrophages, it stimulates the production of NO and the release of TNF-α following IFN-γ activation. MIF likely acts through CD74 and CD44 in a trimeric interaction. Human MIF is active on mouse cells and shares 90%, 94%, 95%, and 90% amino acid identity with mouse, bovine, porcine, and rat MIF, respectively. |
