MIF Human His N

Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus
Cat. No.
BT23056
Source
Escherichia Coli.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Appearance
Sterile filtered colorless solution.
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 40 a.a. His-tag at N-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 ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

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. Notably, MIF is released from macrophages and T cells in response to physiological glucocorticoid concentrations, a unique characteristic. Its secretion is tightly regulated and decreases at high steroid concentrations, which exert anti-inflammatory effects.
Description
Recombinant human MIF, with a 40 a.a. His-tag fused at the N-terminus, was cloned into an E. coli expression vector and purified to apparent homogeneity using standard column chromatography methods. This Macrophage Inducing Factor Human Recombinant (1-115 a.a.) consists of a single, non-glycosylated polypeptide chain with a total of 155 amino acids and a molecular mass of 17kDa.
Physical Appearance
A clear, colorless, and sterile solution.
Formulation
A solution of 1mg/ml in PBS at pH 7.4.
Stability
Liquid MIF remains stable for 1 week at 4°C but should be stored at or below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

Product Science Overview

Introduction

Macrophage Migration Inhibitory Factor (MIF) is a critical cytokine involved in the regulation of the immune response. It was one of the first cytokines to be discovered and has since been recognized for its role in various physiological and pathological processes. The recombinant form of human MIF, tagged with a His-tag at the N-terminus, is widely used in research to study its functions and interactions.

Structure and Expression

The recombinant human MIF is typically expressed in insect cells and purified to high homogeneity. It is a 15 kDa protein consisting of 124 amino acid residues, including an N-terminal His-tag . The His-tag facilitates purification and detection of the protein. The protein is lyophilized and can be reconstituted in water for experimental use .

Biological Functions

MIF plays a multifaceted role in the immune system. It acts as a pro-inflammatory cytokine and an enzyme. MIF’s pro-inflammatory activity is mediated through its interaction with receptors such as CD74 and CD44, leading to the secretion of various cytokines like TNF-α, IL-1, IL-6, and IL-8 . Additionally, MIF has enzymatic activity, functioning as a tautomerase that catalyzes the keto-enol isomerization of substrates like phenylpyruvate and L-dopachrome .

Mechanism of Action

MIF is released from immune cells in response to glucocorticoids, counteracting their immunosuppressive effects. This counter-regulatory mechanism is crucial for maintaining immune homeostasis. MIF also inhibits the random migration of macrophages, hence its name . The protein’s enzymatic activity is dependent on its trimeric configuration and the presence of a free N-terminal proline residue .

Applications in Research

Recombinant human MIF with an N-terminal His-tag is extensively used in research to study its biological functions and interactions. It is employed in various assays to investigate its role in inflammation, immune response, and disease pathogenesis. The His-tag allows for easy purification and detection, making it a valuable tool in molecular biology and biochemistry .

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