TNFA Mouse, Sf9

Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9

Recombinant Mouse TNFA, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 162 amino acids (80-235 a.a.). With a molecular mass of 18 kDa, it appears as a band at approximately 18-28 kDa on SDS-PAGE. This TNFA protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26063
Source
Sf9, Baculovirus cells.
Appearance
Sterile, colorless solution.

TNFA Rat, His Active

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

Recombinant Rat TNFA, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 181 amino acids (spanning positions 80-235). With a molecular mass of 19.9 kDa, this TNFA variant is expressed with a 25 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26165
Source
Escherichia Coli.
Appearance
A clear, colorless liquid that has been sterilized by filtration.

TNFR2 Mouse

Tumor Necrosis Factor Receptor Type 2 Mouse Recombinant

Recombinant TNFR2 Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 236 amino acids. It has a molecular weight of 25.3 kDa. The purification of TNFR2 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27126
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

TNFRSF10A Human Fc

TRAIL Receptor-1 Human Recombinant Fc

Recombinant human TRAIL R1 Fc (amino acids 24-240) is produced in E. coli. This non-glycosylated protein forms a disulfide-linked homodimer, with each chain comprising 217 amino acids. The molecular weight of each chain, including the tag, is 41 kDa. TRAILR1 is fused to a 236 amino acid Fc tag at its C-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27212
Source
Escherichia Coli.
Appearance
The product is supplied as a sterile, white, lyophilized powder.

TNFRSF10B Human

TNF Ligand Receptor Superfamily Member 10B Human Recombinant

Recombinant human TNFRSF10B, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 132 amino acids. It has a molecular weight of 14.8 kDa. The purification of TNFRSF10B is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27288
Source
Escherichia Coli.
Appearance
White, sterile-filtered powder, lyophilized (freeze-dried).

TNFRSF10B Human, Sf9

TNF Ligand Receptor Superfamily Member 10B Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, TNFRSF10B is a single, glycosylated polypeptide chain with a molecular weight of 43.9 kDa. It comprises 394 amino acids (56-210a.a.). On SDS-PAGE, its molecular size appears within the range of 40-57 kDa. The protein is expressed with a C-terminal 239 amino acid hIgG-His tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27339
Source

Sf9, Insect cells.

Appearance
The product is a sterile, colorless solution that has been filtered for clarity.

TNFRSF4 Mouse

TNF Receptor Superfamily Member 4 Mouse Recombinant

Recombinant TNFRSF4 from mice, produced in HEK293 cells, is a single-chain polypeptide with glycosylation. It encompasses amino acids 20 to 211, resulting in a protein of 435 amino acids with a molecular weight of 48.6 kDa. The TNFRSF4 protein is fused with a 243 amino acid hIgG-His tag at its C-terminus. Purification is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT28626
Source

HEK293 cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

TNFRSF6B Human

Tumor Necrosis Factor Receptor Superfamily, Member 6b Human Recombinant

Recombinant human TNFRSF6B, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 294 amino acids (30-300aa). With a molecular weight of 32.1kDa, this protein is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28705
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

TNFRSF8 Human

CD30 Ligand Receptor Human Recombinant

TNFRSF8, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 370 amino acids (19-379 a.a.). It has a molecular mass of 39.5 kDa and migrates at 40-57 kDa on SDS-PAGE under reducing conditions. This TNFRSF8 protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28746
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.

TNFRSF8 igG-His Human

CD30 Ligand Receptor, IgG-His Tag Human Recombinant

TNFRSF8, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular mass of 66.7kDa. It comprises 613 amino acids (19-379 a.a.). On SDS-PAGE, the molecular size appears between 25-100kDa. TNFRSF8 is expressed with a 252 amino acid hIgG-His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28829
Source
Sf9, Baculovirus cells.
Appearance
Colorless, sterile-filtered solution.
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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