IFN tau Ovine

IFN-Tau Ovine Recombinant
Cat. No.
BT26940
Source
Escherichia Coli.
Synonyms

IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Purity
Greater than 95.0% as determined by both:
(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

IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.
The IFN-Tau is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interferon tau (IFN-tau), also referred to as trophoblast protein-1 (TP-1), is classified as a type I IFN. It is produced by trophoblast cells and plays a crucial role in maternal recognition of pregnancy in sheep. IFN-tau exhibits potent immunosuppressive and antiviral properties, similar to other type I IFNs, but with lower cytotoxicity compared to IFN-alpha and IFN-beta. This study investigates the impact of recombinant ovine IFN-tau (rOIFN-tau) on the regulation of MHC class I and II expression in cloned mouse cerebrovascular endothelial (CVE) cells. IFN-tau was observed to induce tyrosine phosphorylation of Stat1 and enhance MHC class I expression on CVE cells. One proposed mechanism through which type I IFNs reduce relapse rates in multiple sclerosis (MS) involves the suppression of IFN-gamma-mediated MHC class II expression. The study revealed that IFN-tau downregulated IFN-gamma-induced MHC class II expression on CVE cells, suggesting its potential therapeutic benefit in mitigating central nervous system (CNS) inflammation. Notably, IFN-tau did not increase MHC class II expression on CVE cells. Furthermore, IFN-tau effectively inhibited Theiler's virus replication in CVE cells.
Description
Recombinant Ovine IFN-Tau, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 172 amino acids. It has a molecular weight of 19914.7 Daltons. The purification process of IFN-Tau involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a solution containing PBS at pH 7.4 with a concentration of 1 mg/ml.
Solubility
To reconstitute the lyophilized IFN Tau, it is recommended to dissolve it in sterile 18 megaohm-centimeter (MΩ·cm) H2O at a concentration of not less than 100 μg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized IFN-Tau remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. Once reconstituted, IFN-Tau should be stored at 4°C for 2-7 days. For extended storage, it is advisable to store it below -18°C. To ensure optimal stability during long-term storage, adding a carrier protein like 0.1% HSA or BSA is recommended. It is important to avoid repeated freeze-thaw cycles.
Purity
The purity of IFN-Tau is greater than 95.0%, as determined by both reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The specific activity of IFN-Tau, assessed using a viral resistance assay with bovine kidney MDBK cells, is 10,000,000 IU/mg.
Synonyms

IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.

Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.

Product Science Overview

Discovery and Significance

IFN-τ was discovered as a unique interferon due to its role in pregnancy recognition in sheep. Unlike other type I interferons, IFN-τ has potent immunosuppressive and antiviral activities but is less cytotoxic . This makes it a promising candidate for therapeutic applications, particularly in modulating immune responses and treating viral infections.

Recombinant Production

The recombinant form of ovine IFN-τ (rOvIFN-τ) is produced using genetic engineering techniques. The gene encoding IFN-τ is cloned and expressed in a suitable host, such as Escherichia coli (E. coli), to produce large quantities of the protein. The process involves several steps :

  1. Gene Cloning: The IFN-τ gene is extracted from sheep embryonic tissues and amplified using reverse transcription-polymerase chain reaction (RT-PCR).
  2. Vector Construction: The amplified gene is inserted into a plasmid vector, such as pET-32a (+), which is then introduced into E. coli cells.
  3. Protein Expression: The E. coli cells are induced to express the recombinant protein using isopropyl-beta-D-thiogalactopyranoside (IPTG).
  4. Protein Purification: The expressed protein is purified using techniques like nickel affinity chromatography and DEAE anion exchange chromatography to obtain a high-purity product.
Biological Activities

Recombinant ovine IFN-τ exhibits several biological activities, including :

  • Immunomodulation: It modulates the expression of major histocompatibility complex (MHC) class I and II molecules, which are crucial for immune responses.
  • Antiviral Activity: It inhibits the replication of viruses, such as vesicular stomatitis virus (VSV) and Theiler’s virus, in various cell types.
  • Anti-inflammatory Effects: It downregulates the expression of MHC class II molecules induced by interferon-gamma (IFN-γ), which may help in reducing inflammation in the central nervous system (CNS).
Potential Therapeutic Applications

Due to its unique properties, recombinant ovine IFN-τ has potential therapeutic applications in various fields :

  • Pregnancy Support: It can be used to support pregnancy in livestock by enhancing maternal recognition of pregnancy.
  • Immune Modulation: Its immunosuppressive properties make it a candidate for treating autoimmune diseases and reducing inflammation.
  • Antiviral Therapy: Its antiviral activity can be harnessed to develop treatments for viral infections.

In conclusion, IFN-τ is a unique and versatile interferon with significant potential for therapeutic applications. Its recombinant production allows for large-scale availability, making it a valuable tool for research and clinical use.

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