TNF a Mouse
Tumor Necrosis Factor-Alpha Mouse Recombinant
Cat. No.
BT25046
Source
Escherichia Coli.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(c) Analysis 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.
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Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton.
The TNF-alpha is purified by standard chromatographic techniques.
The TNF-alpha is purified by standard chromatographic techniques.
Product Specs
Introduction
Tumor necrosis factor (TNF) is a cytokine that plays a crucial role in systemic inflammation and belongs to a group of cytokines that trigger the acute phase reaction. Primarily secreted by macrophages, TNF exerts pleiotropic effects on cells, including the induction of apoptotic cell death, stimulation of cellular proliferation and differentiation, modulation of inflammation, involvement in tumorigenesis and viral replication, regulation of lipid metabolism, and participation in coagulation. Notably, TNF's primary function lies in the regulation of immune cells. Dysregulation and, particularly, excessive production of TNF have been implicated in the pathogenesis of various human diseases, including autoimmune disorders, insulin resistance, and cancer.
Description
Tumor Necrosis Factor-alpha Mouse Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 157 amino acids. With a molecular mass of 17.3 kDa, this recombinant protein is purified using standardized chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.2.
Solubility
To reconstitute the lyophilized Tumor Necrosis Factor-alpha, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions.
Stability
Lyophilized Tumor Necrosis Factor-alpha exhibits stability at room temperature for up to 3 weeks; however, it is advisable to store it desiccated below -18°C. Upon reconstitution, TNF-alpha should be stored at 4°C for a period of 2-7 days. For long-term storage, freezing below -18°C is recommended. To enhance stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. To maintain optimal protein integrity, it is essential to minimize freeze-thaw cycles.
Purity
The purity of the protein is determined using rigorous analytical techniques, including RP-HPLC and SDS-PAGE analysis, and is consistently found to be greater than 97%.
Biological Activity
The biological activity of the protein, as determined by its ability to induce cytolysis in murine L929 cells in the presence of Actinomycin D, is exceptionally high. The ED50 value, a measure of potency, is less than 0.1 ng/ml, which translates to a Specific Activity of 10,000,000 Units/mg.
Protein Content
Protein quantification is performed using two independent and reliable methods: 1) UV spectroscopy at 280 nm, employing an absorbency value of 1.24 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is derived from the PC GENE computer analysis program, which is specifically designed for analyzing protein sequences (IntelliGenetics). 2) Analysis by RP-HPLC, utilizing a precisely calibrated solution of TNF-alpha as a Reference Standard.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Source
Escherichia Coli.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Product Science Overview
Discovery and Structure
TNF-α was originally discovered in 1975 as a macrophage cytotoxic factor capable of killing mouse fibrosarcoma L-929 cells, leading to its name "tumor necrosis factor" . The gene encoding TNF-α is located on chromosome 6p21.3 and comprises four exons . The precursor form of TNF-α, known as pro-TNF-α, is a type II transmembrane protein with a molecular weight of 26 kDa. This precursor consists of mature TNF-α and a leader sequence, which includes a cytoplasmic domain, a transmembrane domain, and an extracellular domain .
Biological Functions
TNF-α is involved in various biological processes, including:
- Immunomodulation: It regulates immune responses by influencing the activity of various immune cells.
- Inflammatory Response: TNF-α is a key mediator of inflammation, initiating the cascade of other cytokines and factors that constitute the immune system’s response to infection and cancer .
- Cell Survival and Apoptosis: TNF-α can induce apoptosis (programmed cell death) in certain tumor cells, contributing to its anti-tumorigenic properties .
- Fever Induction: It plays a role in the development of fever during infections.
- Inhibition of Tumor Formation and Viral Replication: TNF-α has been shown to inhibit the formation of tumors and the replication of viruses .
Recombinant TNF-α
Recombinant TNF-α, particularly the mouse version, is produced using various expression systems, including Escherichia coli (E. coli). This recombinant form retains the biological activities of the native protein and is used in research to study its effects on immune responses, inflammation, and cancer .
Applications in Research
Recombinant TNF-α is widely used in scientific research to:
- Investigate the mechanisms of immune regulation and inflammation.
- Study the effects of TNF-α on tumor cells and its potential as an anti-cancer agent.
- Explore its role in various diseases, including autoimmune disorders and infectious diseases.
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