IFNG Human, His Active

Interferon-gamma Human Recombinant, His Tag Active
Cat. No.
BT27963
Source
Escherichia Coli.
Synonyms

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Appearance
Sterile Filtered colorless liquid.
Purity

Greater than 90.0% as determined 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

IFNG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) and having a molecular mass of 18.4kDa. IFNG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
IFN-gamma is produced by lymphocytes that are activated by specific antigens or mitogens. This cytokine has important immunoregulatory functions in addition to antiviral activity. IFN-gamma is a potent activator of macrophages, has antiproliferative effects on transformed cells, and can potentiate the antiviral and antitumor effects of type I interferons.
Description
Recombinant human IFNG produced in E. coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (24-161 a.a). This protein has a molecular mass of 18.4 kDa. The N-terminus of IFNG is fused to a 21 amino acid His-tag. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Colorless, sterile filtered liquid
Formulation
IFNG protein solution (1 mg/ml) in phosphate buffered saline (pH 7.4) and 20% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For longer-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid multiple freeze-thaw cycles.
Purity
Greater than 90.0% purity as determined by SDS-PAGE.
Biological Activity
Biological activity is measured in a cytotoxicity assay using WiDr cells. The ED50 for this effect is approximately 5 ng/ml.
Synonyms

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

Product Science Overview

Introduction

Interferon-gamma (IFN-γ) is a dimerized soluble cytokine and the only member of the type II class of interferons. It plays a crucial role in the immune system by inhibiting viral replication directly and through its immunostimulatory and immunomodulatory effects . Human recombinant IFN-γ, particularly with a His tag, is a form of this cytokine that has been engineered for research and therapeutic purposes.

Structure and Expression

Recombinant human IFN-γ is typically produced in various expression systems, such as HEK293 cells or E. coli. The His tag, a sequence of histidine residues, is added to facilitate purification through affinity chromatography. This recombinant protein is often expressed as a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of approximately 18.4 kDa .

Biological Activity

IFN-γ is known for its broad-spectrum antiviral properties. It is produced by lymphatic T cells and natural killer cells upon stimulation by antigens . The cytokine activates effector immune cells and enhances antigen presentation, making it a vital component in the body’s defense against infections and tumors . Recombinant IFN-γ retains these biological activities, making it a valuable tool in clinical research and therapeutic applications.

Preparation Methods

The production of recombinant human IFN-γ involves several steps:

  1. Gene Cloning: The gene encoding human IFN-γ is cloned into an expression vector.
  2. Transformation: The vector is introduced into a suitable host cell line, such as HEK293 or E. coli.
  3. Expression: The host cells are cultured under conditions that promote the expression of the recombinant protein.
  4. Purification: The His tag allows for easy purification of the protein using affinity chromatography techniques.
  5. Validation: The purity and biological activity of the recombinant protein are validated through various assays, such as SDS-PAGE and functional assays .
Applications

Recombinant human IFN-γ is used in various research and clinical applications, including:

  • Antiviral Research: Studying the mechanisms of viral inhibition and developing antiviral therapies.
  • Cancer Research: Investigating the role of IFN-γ in tumor suppression and developing immunotherapies.
  • Immunology: Understanding the modulation of immune responses and the enhancement of antigen presentation .

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