Product List

LTBR Human

Lymphotoxin Beta Receptor Human Recombinant

LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.
LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24218
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TNFRSF8 Mouse

CD30 Ligand Receptor Mouse Recombinant

TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.
TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28913
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

TNFSF12 Human

TNF Ligand Superfamily Member 12 Human Recombinant

TNFSF12 Human Recombinant (94-249 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a total molecular mass of 18kDa.

The TNFSF12 is fused with an 8 amino acids his tag at N-terminal (M-HHHHHH-R, total 164 a.a.) and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT29016
Source

Escherichia coli.

Appearance
Filtered White lyophilized (freeze-dried) powder.

TNFSF14 Human

LIGHT Human Recombinant

Recombinant Human LIGHT (74-240 aa) having a Mw of 23kDa was purified from E. coli.
The Recombinant Human LIGHT is purified by proprietary chromatographic technique.

Shipped with Ice Packs
Cat. No.
BT29066
Source

Escherichia Coli.

Appearance

Sterile Filtered clear solution.

TNFSF14 Mouse

LIGHT Mouse Recombinant

TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.
Shipped with Ice Packs
Cat. No.
BT29148
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Mouse OX40L

OX40 Ligand Mouse Recombinant

OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.
OX40L  is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24297
Source

Sf9, Baculovirus cells.

Appearance

Sterile filtered colorless solution.

OX40L Human

OX40 Ligand Human Recombinant

OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa.
OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24383
Source

HEK293 Cells.

Appearance

Sterile Filtered colorless solution.

RANK Mouse

RANK Mouse Recombinant

RANK Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 426 amino acids (31-214 aa) and having a molecular mass of 47.5kDa.
RANK is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24426
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

RELT Human

RELT Human Recombinant

RELT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 376 amino acids (26-162a.a.) and having a molecular mass of 41.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
RELT 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.
BT24515
Source

Sf9, Baculovirus cells.

Appearance
Sterile filtered colorless solution.

TACI Human, Sf9

Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9

TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.


Shipped with Ice Packs
Cat. No.
BT24574
Source
Sf9, Insect cells.
Appearance
Sterile filtered colorless 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.
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