MIF Human His C

Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus
Cat. No.
BT22974
Source
Escherichia Coli.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Appearance
Sterile Filtered lyophilized powder.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

MIF human Recombinant, fused to His-tag at C-terminus, 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 chaincontaining 123 amino acidsand having a molecular mass of 13.5 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 physiological concentrations of glucocorticoids. Its secretion is tightly regulated and decreases at high, anti-inflammatory steroid concentrations.
Description
Recombinant human MIF, with a His-tag fused at the C-terminus, was cloned into an E. coli expression vector and purified to apparent homogeneity using standard column chromatography techniques. This human recombinant Macrophage Inducing Factor is a single, non-glycosylated polypeptide chain comprising 123 amino acids with a molecular weight of 13.5 kDa.
Physical Appearance
Sterile filtered powder in lyophilized form.
Formulation
Human MIF was lyophilized from a solution of 1mg/ml in PBS with a pH of 7.4.
Solubility
To reconstitute the lyophilized MIF, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration not less than 100µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized MIF remains stable at room temperature for up to 3 weeks. However, for long-term storage, it should be stored desiccated below -18°C. Once reconstituted, MIF should be stored at 4°C for 2-7 days. For future use, store below -18°C. To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using the following methods: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis and (b) SDS-PAGE analysis.
Biological Activity
Biological activity is assessed based on its ability to bind to rhCD74 in a functional ELISA assay.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Source
Escherichia Coli.
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.

Product Science Overview

Introduction

Macrophage Migration Inhibitory Factor (MIF) is a small, secreted protein that plays a crucial role in the immune system. It acts as a pro-inflammatory cytokine and an enzyme, influencing various immune responses. The recombinant form of MIF, particularly the human recombinant with a His tag at the C-terminus, is widely used in research to study its functions and potential therapeutic applications.

Structure and Expression

Human recombinant MIF is typically expressed in insect cells and purified to high levels of purity, often exceeding 98% as determined by SDS-PAGE and HPLC analyses . The recombinant protein is a 15 kDa molecule containing 124 amino acid residues, including an N-terminal His-tag . This His-tag facilitates purification and detection of the protein in various experimental setups.

Biological Functions

MIF is known for its dual role as a cytokine and an enzyme. As a cytokine, MIF is involved in the regulation of immune responses. It is secreted by various cells, including macrophages and T cells, in response to inflammatory stimuli. MIF binds to receptors such as CD74 and CD44 on target cells, triggering the release of other pro-inflammatory cytokines like tumor necrosis factor-alpha (TNF-α), interleukins (IL-1, IL-6, IL-8), and matrix metalloproteinases (MMPs) .

As an enzyme, MIF exhibits tautomerase activity, catalyzing the keto-enol isomerization of substrates like keto-phenylpyruvate and L-dopachrome . This enzymatic activity is dependent on its trimeric configuration and the presence of a free N-terminal proline residue .

Role in Disease

MIF has been implicated in various diseases due to its pro-inflammatory properties. It plays a significant role in conditions such as sepsis, autoimmune diseases, and cancer. Elevated levels of MIF have been observed in patients with these conditions, making it a potential target for therapeutic interventions .

Recombinant MIF in Research

The human recombinant MIF with a His tag at the C-terminus is a valuable tool in research. It allows scientists to study the protein’s structure, function, and interactions in detail. The His tag aids in the purification process, ensuring that high-purity protein is available for experiments. Additionally, recombinant MIF is used in assays to investigate its role in immune responses and its potential as a therapeutic target .

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