TNFA Bovine

Tumor Necrosis Factor-alpha Bovine Recombinant

TNFA Bovine produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (78-234 a.a.) and having a molecular mass of 17.5kDa.

TNFA is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT25984
Source

Escherichia Coli.

Appearance

Sterile filtered colorless solution.

TNFA Mouse, Sf9

Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9

TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26063
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

TNFA Rat, His Active

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.
TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26165
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid.

TNFAIP8 Human

Tumor Necrosis Factor, Alpha-Induced Protein 8 Human Recombinant

TNFAIP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-198a.a.) and having a molecular mass of 25kDa. TNFAIP8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26253
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TNFR (22-211) Human

Tumor Necrosis Factor Receptor (22-211 a.a.) Human Recombinant

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (22-211 a.a) and having a molecular mass of 23.6kDa.
TNFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26320
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TNFR Human

Tumor Necrosis Factor Receptor Human Recombinant

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids and having a total molecular mass of 18.2 kDa. TNFR Human Recombinant is purified by 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

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 161 amino acids fragment (41-201) having a molecular weight of 22.68kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR His Tag is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26480
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

TNFR Human, Sf9

Tumor Necrosis Factor Receptor, sf9 Human Recombinant

TNFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (18-186 a.a.) and having a molecular mass of 45.3kDa. (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
TNFR is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26545
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

TNFR Mouse

Tumor Necrosis Factor Receptor Mouse Recombinant

TNFR Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.1kDa.
The TNFR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26637
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TNFR2 Human

Tumor Necrosis Factor Receptor Type 2 Human Recombinant

TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26785
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
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