Cytokines
Product List
TNFR (22-211) Human
Tumor Necrosis Factor Receptor (22-211 a.a.) Human Recombinant
TNFRSF10C Human
TRAIL Receptor-3 Human Recombinant
TNFRSF10D Human
TRAIL Receptor-4 Human Recombinant
Produced using Sf9 Baculovirus cells, TNFRSF10D is a single, glycosylated polypeptide chain consisting of 395 amino acids (specifically, residues 56-211a.a.). It has a molecular mass of 73.8kDa. However, on SDS-PAGE, the apparent molecular size may fall within the range of 40-57kDa.
TNFRSF10D is expressed with a C-terminal 239 amino acid hIgG-His tag and purified through proprietary chromatographic techniques.
TNFRSF12A Human
TNF Ligand Receptor Superfamily Member 12A Human Recombinant
TNFRSF12A Human, sf9
TNF Ligand Receptor Superfamily Member 12A Human Recombinant, Sf9
Recombinant human TNFRSF12A, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein comprises 292 amino acids (residues 28-80a.a.) and has a molecular mass of 32.6 kDa. Notably, on SDS-PAGE, it appears at a size of approximately 28-40 kDa. This discrepancy arises from glycosylation and the presence of a 239-amino acid hIgG-His tag at the C-terminus. The protein undergoes purification using proprietary chromatographic techniques.
Sf9, Baculovirus cells.
TNFRSF14 Human
HVEM-Fc Human Recombinant
TNFRSF8 Mouse
CD30 Ligand Receptor Mouse Recombinant
Sf9, Baculovirus cells.
TNFSF12 Human
TNF Ligand Superfamily Member 12 Human Recombinant
Recombinant Human TNFSF12 (amino acids 94-249) produced in E. coli results in a single, non-glycosylated polypeptide chain. With a molecular mass of 18 kDa, it comprises 156 amino acids. An 8-amino acid histidine tag (M-HHHHHH-R) is fused to the N-terminus, resulting in a total of 164 amino acids. Purification is achieved using proprietary chromatographic techniques.
Escherichia coli.
TNFSF14 Human
LIGHT Human Recombinant
TNFSF14 Mouse
LIGHT Mouse Recombinant
Introduction
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.
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.
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.
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:
- 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.
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 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.
