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TNF a Human, HEK

Tumor Necrosis Factor-alpha Human Recombinant, HEK

 
Catalog #
CYK0663
Uniprot Id
P01375
 
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CYK0663-2 7 days 2 µg $120.00
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CYK0663-10 7 days 10 µg $290.00
CYK0663-1 7 days 1 mg $8,320.00
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Product Overview

NameTNF a Human, HEK
Description
Tumor Necrosis Factor-alpha Human Recombinant, HEK
Accession (Primary)P01375
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.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein was lyophilized with no additives.
Stability
Lyophilized Tumor Necrosis Factor-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 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Amino acid sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Ser-Ser.
Biological Activity
The ED50 as determined by the cytotoxicity of porcine PK15 cells was found to be 0.001-0.015 ng/ml.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 1.26 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.
Precautions
TNF a Human, HEK is for research use only and not for use in diagnostic or therapeutic procedures.

Target Information: ( P01375 )

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

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

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