prospec
TNF a Human, HEK

TNF a Human, HEK

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  • Description
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  • Quantity
  • TNF a Human, HEK

  • Tumor Necrosis Factor-alpha Human Recombinant, HEK
  • CYT-114
  • Shipped at Room temp.

Catalogue number

CYT-114

Synonyms

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Introduction

Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

Description

TNF-a Human Recombinant produced in HEK cells is a glycosylated non-disulfide linked homotrimer, containing 157 and having total Mw of 17kDa.
The TNF-a is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

The TNF-a protein was lyophilized from 1mg/ml in 1xPBS.

Solubility

It is recommended to reconstitute the lyophilized TNF-a in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized TNF-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent cytotoxity of the TNF alpha sensitive cell line L-929 in the presence of Actinomycin D and is typically 0.05-0.5ng/ml.

Amino acid sequence

VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLI
YSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYL
GGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL.

Safety Data Sheet

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Background

Tumor Necrosis Factor-alpha Human Recombinant, HEK: An In-Depth Analysis

 

Abstract: Tumor Necrosis Factor-alpha (TNF-α) is a potent cytokine involved in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Human Recombinant produced in Human Embryonic Kidney (HEK) cells, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of TNF-α modulation in human diseases.

 

Introduction:

 

TNF-α is a key mediator of immune responses and inflammation in humans. This paper aims to provide a comprehensive analysis of TNF-α Human Recombinant produced in HEK cells, highlighting its significance in human physiology and its potential therapeutic applications.

 

Structure and Function of TNF-α:

 

TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.

 

Signaling Pathways:

 

Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, affecting inflammation, apoptosis, and tissue homeostasis.

 

Functions of TNF-α:

 

TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of inflammatory and autoimmune diseases, making it an attractive therapeutic target.

 

Therapeutic Potential:

 

TNF-α modulation has revolutionized the treatment of inflammatory diseases. TNF-α inhibitors, such as monoclonal antibodies and soluble receptors, have shown efficacy in conditions like rheumatoid arthritis, psoriasis, and inflammatory bowel disease. TNF-α-based therapies are being explored for their potential in cancer treatment and immunotherapy.

 

Future Directions:

 

Further research is required to enhance our understanding of TNF-α signaling and its interactions with other molecular pathways in human diseases. Future directions involve personalized medicine approaches, identifying predictive biomarkers, and developing targeted therapies that optimize the therapeutic potential of TNF-α modulation.

References

  1. Aggarwal, B. B. (2003). Signalling pathways of the TNF superfamily: A double-edged sword. Nature Reviews Immunology, 3(9), 745-756.
  2. Tracey, D., et al. (2008). Anti-TNF therapy: Past, present, and future. EXS, 102, 105-117.
  3. Feldmann, M., et al. (2018). Biological insights from clinical trials with anti-TNF therapy. Seminars in Immunology, 28(2), 139-147.
  4. Kalliolias, G. D., & Ivashkiv, L. B. (2016). TNF biology, pathogenic mechanisms, and emerging therapeutic strategies. Nature Reviews Rheumatology, 12(1), 49-62.
  5. McInnes, I. B., & Schett, G. (2011). Cytokines in the pathogenesis of rheumatoid arthritis. Nature Reviews Immunology, 7(6), 429-442.
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