Growth Factors
CD Antigens
Enzymes
Viral Antigens
Recombinant Proteins
Natural Proteins
Monoclonal Antibodies
Cytokines
Polyclonal Antibodies
Neurotrophins
Chemokines
Hormones
Custom Antibodies
Modified Histone Antibodies
Tag/Control Antibodies
Antibody Pairs
Secondary Antibodies
Small Molecular Antibodies
Recombinant Antibodies
ChIP Antibodies
Cytokines
Product List
TNFRSF4 Human
TNF Receptor Superfamily Member 4 Human Recombinant
Produced in Sf9 insect cells, TNFRSF4 is a single, glycosylated polypeptide chain with a molecular weight of 46.9 kDa (although it may appear between 40-57 kDa on SDS-PAGE). This recombinant protein encompasses amino acids 29-214 and includes a 239 amino acid IgG-His tag at the C-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT28559
Source
Sf9,
Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.
TNF a Rat, His
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag
Recombinant Rat TNF alpha, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 181 amino acids (80-235 a.a.). It possesses a molecular mass of 19.9 kDa. This TNF alpha variant is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
TNF a Rhesus Macaque
Tumor Necrosis Factor-Alpha Rhesus Macaque Recombinant
Recombinant TNF-alpha from Rhesus Macaque, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 157 amino acids, with a molecular weight of 17.3 kDa. The purification of TNF-alpha from Rhesus Macaque is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25463
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered.
TNF alpha human
Tumor Necrosis Factor-Alpha Human Recombinant
Recombinant Human Tumor Necrosis Factor-alpha produced in E. coli is a single polypeptide chain, lacking any sugar modifications (non-glycosylated), and consists of 158 amino acids. This includes 157 amino acids of the mature human TNF-alpha protein and an additional methionine at the beginning of the chain (N-terminal). It has a molecular weight of 17.5kDa.
The purification of TNF-alpha is achieved through a series of standard chromatographic separation techniques.
The purification of TNF-alpha is achieved through a series of standard chromatographic separation techniques.
Shipped with Ice Packs
Cat. No.
BT25546
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
TNF b Human
Tumor Necrosis Factor-Beta Human Recombinant
Recombinant Human Tumor Necrosis Factor-beta (Lymphotoxin) is produced in E. coli. This non-glycosylated polypeptide consists of 172 amino acids, resulting in a molecular weight of 18645 Daltons. The purification process of TNF-b involves standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25623
Source
Escherichia Coli.
Appearance
The product appears as a sterile, white lyophilized (freeze-dried) powder.
TNFR Human
Tumor Necrosis Factor Receptor Human Recombinant
Recombinant human TNFR, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 162 amino acids with a molecular mass of 18.2 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26417
Source
Escherichia Coli.
Appearance
Sterile filtered white lyophilized (freeze-dried) powder.
TNFR Human, His
Tumor Necrosis Factor Receptor Type Human Recombinant, His Tag
Recombinant Human TNFR, produced in E. coli, is an unglycosylated polypeptide chain (161 amino acids). This fragment (amino acids 41-201) has a molecular weight of 22.68 kDa and includes a 4.5 kDa N-terminal hexahistidine tag. Purification of the TNFR His Tag is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26480
Source
Escherichia Coli.
Appearance
A clear solution, sterilized by filtration.
TNFR Human, Sf9
Tumor Necrosis Factor Receptor, sf9 Human Recombinant
Produced in Sf9 Baculovirus cells, TNFR is a single, glycosylated polypeptide chain comprising 411 amino acids (specifically, amino acids 18-186). It has a molecular mass of 45.3 kDa and migrates at 40-57 kDa on SDS-PAGE under reducing conditions.
Shipped with Ice Packs
Cat. No.
BT26545
Source
Sf9,
Baculovirus cells.
Appearance
The product is a sterile, colorless, and filtered solution.
TNFR Mouse
Tumor Necrosis Factor Receptor Mouse Recombinant
Recombinant Mouse TNFR, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 191 amino acids with a molecular weight of 21.1 kDa. The purification of TNFR is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26637
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.
TNFRSF14 Human, His
HVEM Human Recombinant, His Tag
Recombinant human TNFRSF14, produced in E. Coli, is a single glycosylated polypeptide chain containing 187 amino acids (39-202) with a molecular weight of 19.7 kDa. It consists of the TNFRSF14 protein fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
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.
