TNF b Human, His

Tumor Necrosis Factor-Beta Human Recombinant, His Tag
Cat. No.
BT25711
Source
Escherichia Coli.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
Prospec'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

TNF-b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (35-205 a.a.) and having a molecular mass of 20.9kDa.
TNF-b is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tumor necrosis factor beta (TNF-β), also known as lymphotoxin, is a potent cytokine primarily produced by activated T lymphocytes and B lymphocytes. It exhibits cytotoxic activity against various target cells, including tumor cells, and plays a crucial role in inflammation and immune responses.
Description
Recombinant human TNF-β, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 192 amino acids (residues 35-205). It has a molecular weight of 20.9 kDa. The protein includes a 21 amino acid His-tag at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The TNF-β protein solution is provided at a concentration of 0.25 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 30% glycerol, 0.1 M NaCl, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For longer storage, it is recommended to freeze the product at -20°C. To ensure stability during long-term storage, adding a carrier protein such as 0.1% HSA or BSA is advised. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the protein is determined to be greater than 90% by SDS-PAGE analysis.
Biological Activity
The biological activity of TNF-β is evaluated based on its cytotoxic effect on L929 mouse fibrosarcoma cells in the presence of actinomycin D, a metabolic inhibitor. The ED50 value, representing the concentration of TNF-β required to achieve 50% cell death, is determined to be less than 0.3 ng/ml.
Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.

Product Science Overview

Introduction

Tumor Necrosis Factor-Beta (TNF-β), also known as Lymphotoxin-alpha (LT-α), is a cytokine that plays a crucial role in the regulation of immune responses and inflammation. It is a member of the tumor necrosis factor superfamily, which includes other well-known cytokines such as Tumor Necrosis Factor-Alpha (TNF-α). TNF-β is produced by lymphocytes and exhibits cytotoxic activity against tumor cells, making it a significant molecule in cancer research and immunotherapy .

Structure and Expression

The human recombinant form of TNF-β, tagged with a His-tag, is a single, non-glycosylated polypeptide chain consisting of 192 amino acids. The His-tag, a sequence of histidine residues, is added to the N-terminus of the protein to facilitate purification through affinity chromatography. This recombinant protein is typically expressed in Escherichia coli (E. coli) and purified using proprietary chromatographic techniques .

Biological Activity

TNF-β functions as a soluble homotrimer and can also form heterotrimers with Lymphotoxin-beta (LT-β) when anchored to the cell surface. It exhibits a variety of biological activities, including the induction of cell death in certain tumor cell lines, regulation of immune responses, and involvement in the development of secondary lymphoid organs. TNF-β’s cytotoxic activity is measured using assays such as the cytotoxicity assay with L929 mouse fibrosarcoma cells in the presence of actinomycin D .

Applications in Research

The recombinant form of TNF-β is widely used in research to study its role in immune regulation, inflammation, and cancer. It is utilized in various assays to investigate its cytotoxic effects, signaling pathways, and interactions with other cytokines. The His-tagged version allows for easy purification and detection, making it a valuable tool in biochemical and cellular studies .

Storage and Stability

The recombinant TNF-β protein is typically stored at -20°C for long-term storage, with the addition of carrier proteins such as human serum albumin (HSA) or bovine serum albumin (BSA) to enhance stability. It is recommended to avoid multiple freeze-thaw cycles to maintain the protein’s integrity. For short-term use, the protein can be stored at 4°C .

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