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Product List
TNFSF7 Human
CD70 Human Recombinant
Recombinant human TNFSF7, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 178 amino acids (residues 39-193) and exhibiting a molecular mass of 19.5 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT29206
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
TNFRSF10A Human
TRAIL Receptor-1 Human Recombinant
Produced in Sf9 Baculovirus cells, TNFRSF10A is a single, glycosylated polypeptide chain comprising 224 amino acids (24-239a.a.) with a molecular weight of 23.9 kDa. This protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23980
Source
Sf9,
Baculovirus cells.
Appearance
Sterile, colorless solution.
APRIL Human
APRIL Human Recombinant
Recombinant human APRIL, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 159 amino acids (residues 105-247) with a molecular weight of 17.6 kDa. It includes a 16-amino acid T7 tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24057
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
APRIL Mouse
APRIL Mouse Recombinant
Recombinant Mouse APRIL, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 146 amino acids with a molecular weight of 16.4 kDa. The APRIL protein undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24131
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
LTBR Human
Lymphotoxin Beta Receptor Human Recombinant
Recombinant human LTBR, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 224 amino acids (residues 28-227) and has a molecular weight of 24.6 kDa. This LTBR protein is fused to a 24 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24218
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
TACI Human
Tumor Necrosis Factor Receptor 13B Human Recombinant
Recombinant human TACI produced in E. coli is a single, non-glycosylated polypeptide chain comprising 160 amino acids, resulting in a molecular weight of 18.0kDa.
Shipped with Ice Packs
Cat. No.
BT24650
Source
Escherichia Coli.
Appearance
The product is a sterile, white powder that has been lyophilized (freeze-dried).
TACI Human, His
Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag
Recombinant human TACI protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 188 amino acids (including a 23 amino acid His tag at the N-terminus), encompassing amino acids 1-165 of the native sequence. The protein has a molecular weight of 20.9 kDa and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24706
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.
TNF a Canine
Tumor Necrosis Factor-Alpha Canine Recombinant
Recombinant Canine TNF-a, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 157 amino acids. With a molecular mass of 17.3 kDa, it is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24796
Source
Escherichia Coli.
Appearance
The product appears as a sterile, filtered white powder, freeze-dried for preservation.
TNF a Human, His
Tumor Necrosis Factor-Alpha Human Recombinant, His Tag
Recombinant human Tumor Necrosis Factor-alpha (TNF-α) with a His tag, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein fragment consists of 164 amino acids, has a molecular weight of 18.3 kDa, and includes an N-terminal hexahistidine tag. The purification process of TNF-alpha His involves standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24869
Source
Escherichia Coli.
Appearance
The product appears as a sterile, filtered, and lyophilized (freeze-dried) powder, white in color.
TNF a Human, Sf9
Tumor Necrosis Factor-alpha Human Recombinant, Sf9
Produced in Sf9 insect cells using a baculovirus expression system, this recombinant TNF-alpha protein is a single, glycosylated polypeptide chain comprising 163 amino acids (residues 77-233). It has a molecular weight of 18.1 kDa, but on SDS-PAGE, it appears as a band at approximately 18-28 kDa due to glycosylation. This TNF-alpha variant is engineered with a 6-amino acid His tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24973
Source
Sf9,
Baculovirus cells.
Appearance
The product is a clear, sterile-filtered solution.
Introduction
Definition and Classification
Tumor Necrosis Factor (TNF) is a cytokine, a type of signaling protein involved in systemic inflammation and is part of the body’s immune response. TNF is primarily produced by activated macrophages, although it can also be produced by other cell types such as lymphocytes, natural killer cells, and neurons. TNF is classified into two main forms:
- TNF-α (Tumor Necrosis Factor-alpha): The most studied form, involved in systemic inflammation and acute phase reactions.
- TNF-β (Tumor Necrosis Factor-beta): Also known as lymphotoxin, it is produced by lymphocytes and has similar but distinct functions compared to TNF-α.
Biological Properties
Key Biological Properties:
- Molecular Weight: TNF-α is a 17 kDa protein, while TNF-β is slightly larger.
- Structure: TNF-α is a trimeric protein, meaning it forms a complex of three identical subunits.
Expression Patterns:
- TNF-α: Expressed primarily by macrophages, but also by other immune cells such as T cells and natural killer cells.
- TNF-β: Expressed by activated lymphocytes.
Tissue Distribution:
- TNF is found in various tissues, including the spleen, liver, and adipose tissue. It is also present in the bloodstream during systemic inflammation.
Biological Functions
Primary Biological Functions:
- Inflammation: TNF is a key mediator of inflammation, promoting the recruitment of immune cells to sites of infection or injury.
- Cell Death: TNF can induce apoptosis (programmed cell death) in certain cells, which is crucial for controlling infections and preventing cancer.
- Immune Response: TNF plays a role in the activation and differentiation of immune cells, enhancing the body’s ability to fight off pathogens.
Role in Immune Responses:
- Pathogen Recognition: TNF helps in recognizing and responding to pathogens by activating immune cells and promoting the production of other cytokines.
Modes of Action
Mechanisms with Other Molecules and Cells:
- Receptors: TNF exerts its effects by binding to two receptors, TNFR1 and TNFR2, which are present on the surface of various cells.
- Binding Partners: TNF can interact with other cytokines and signaling molecules to amplify or modulate its effects.
Downstream Signaling Cascades:
- NF-κB Pathway: Activation of TNFR1 leads to the activation of the NF-κB pathway, which promotes the expression of genes involved in inflammation and cell survival.
- MAPK Pathway: TNF can also activate the MAPK pathway, leading to the production of inflammatory mediators.
Regulatory Mechanisms
Regulatory Mechanisms:
- Transcriptional Regulation: The expression of TNF is tightly regulated at the transcriptional level by various transcription factors, including NF-κB and AP-1.
- Post-Translational Modifications: TNF undergoes several post-translational modifications, such as glycosylation and cleavage, which can affect its activity and stability.
Applications
Biomedical Research:
- Disease Models: TNF is used in research to study inflammatory diseases, cancer, and autoimmune disorders.
Diagnostic Tools:
- Biomarkers: Elevated levels of TNF in the blood can serve as biomarkers for various inflammatory and autoimmune diseases.
Therapeutic Strategies:
- Anti-TNF Therapies: Drugs that inhibit TNF, such as infliximab and etanercept, are used to treat conditions like rheumatoid arthritis, Crohn’s disease, and psoriasis.
Role in the Life Cycle
Role Throughout the Life Cycle:
- Development: TNF is involved in embryonic development, particularly in the formation of the immune system.
- Aging: TNF levels can increase with age, contributing to age-related inflammation and diseases.
- Disease: Dysregulation of TNF is associated with various diseases, including chronic inflammatory conditions, cancer, and neurodegenerative disorders.
