MIF Human, Active

Macrophage Migration Inhibitory Factor Human Recombinant (Active)
Cat. No.
BT23136
Source
Escherichia Coli.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.
Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.

Product Specs

Introduction
Macrophage migration inhibitory factor (MIF) is a cytokine secreted by the pituitary gland and monocyte/macrophage cells. It plays a crucial role in endotoxic shock. Uniquely, MIF is released from macrophages and T cells in response to typical physiological levels of glucocorticoids. Its secretion is carefully regulated, decreasing at higher steroid concentrations, which have anti-inflammatory effects.
Description
Recombinant human MIF was produced using an E. coli expression system. Purification to apparent homogeneity was achieved through standard column chromatography methods. This recombinant human Macrophage Inducing Factor is a single, non-glycosylated polypeptide chain composed of 115 amino acids, resulting in a molecular weight of 12.5 kDa.
Physical Appearance
Sterile Filtered White lyophilized powder.
Biological Activity
The biological activity of this recombinant human MIF was assessed using human PBMCs. Cells were exposed to varying concentrations of MIF (0 to 1000 ng/ml), and IL-8 production was measured via ELISA after 24 hours. The ED50 for this effect was determined to be in the range of 88-132 ng/ml.
Formulation
Prior to lyophilization, the MIF protein was prepared in a 10mM sodium phosphate buffer at pH 7.5.
Solubility
To reconstitute the lyophilized MIF protein, it is recommended to use sterile 18MΩ-cm H2O. Aim for a final concentration between 0.1 mg/ml and 1 mg/ml.
Stability
Lyophilized MIF protein demonstrates stability at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store the lyophilized product desiccated at a temperature below -18°C. After reconstitution, the MIF protein solution should be stored at 4°C and used within 2-7 days. For long-term storage of the reconstituted protein, consider adding a carrier protein such as HSA or BSA at a concentration of 0.1%. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of this recombinant human MIF is greater than 97.0%, as determined by two separate analytical methods: Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Source
Escherichia Coli.
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
INYYDMNAANVGWNNSTFA.

Product Science Overview

Discovery and Early Research

MIF was first characterized during studies on delayed-type hypersensitivity reactions, where it was found to inhibit macrophage migration . This discovery highlighted its potential role in immune regulation. Subsequent research revealed that MIF is stored in and secreted from the pituitary gland upon endotoxaemia, acting as a key regulator of innate immunity by counter-regulating glucocorticoids .

Structure and Function

MIF is a pleiotropic cytokine with chemokine-like functions. It is involved in a wide range of cellular processes, including:

  • Inflammation: MIF is a pro-inflammatory cytokine that plays a significant role in the immune response. It is overexpressed in various inflammatory diseases and cancers .
  • Cellular Homeostasis: MIF influences cellular survival, antioxidant signaling, angiogenesis, and tissue repair .
  • Immune Regulation: MIF acts as a negative regulator of glucocorticoid actions, thereby modulating the immune response .
Recombinant MIF

The production of recombinant MIF has enabled more detailed studies of its functions. Recombinant MIF is typically expressed in insect cells and purified for research purposes . This recombinant form retains the biological activity of the native protein and is used in various experimental settings to study its role in disease models.

Therapeutic Potential

Given its involvement in numerous pathological conditions, MIF is considered a potential therapeutic target. Inhibition of MIF signaling has shown promise in restoring anticancer immune responses in tumor microenvironments . Additionally, therapeutic interventions targeting MIF are being explored for their potential to modulate inflammation and tissue repair .

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