TNFR2 Human, His

Tumor Necrosis Factor Receptor Type 2 Human Recombinant, His Tag
Cat. No.
BT26947
Source
Escherichia Coli.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's 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.
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Description

TNFR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 184 amino acids fragment (23-206) having a molecular weight of 24.45kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The TNFR2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
TNFR2, a member of the TNF-receptor superfamily, exhibits a high affinity for TNFSF2/TNF-alpha and a fivefold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. This receptor plays a crucial role in mediating the metabolic effects of TNF-alpha. Studies on knockout mice suggest that TNFR2 protects neurons from apoptosis by activating antioxidative pathways. Furthermore, TNFR2 expression may be implicated in angiogenesis, tumor cell proliferation, and metastasis in invasive micropapillary carcinoma of the breast. Two soluble TNF receptor types, sTNFR-I and sTNFR-II, neutralize the biological activities of TNF-alpha and TNF-beta. These soluble receptors are generated through the shedding of the extracellular domains of membrane-bound receptors, and their levels tend to rise accordingly. Notably, high concentrations of soluble TNF receptors are present in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex that facilitates the recruitment of two anti-apoptotic proteins, c-IAP1 and c-IAP2, both of which possess E3 ubiquitin ligase activity. While the precise function of IAPs in TNF-receptor signaling remains elusive, c-IAP1 is thought to enhance TNF-induced apoptosis by ubiquitinating and degrading TNF-receptor-associated factor 2, a protein that mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, leading to ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1, and TNFR2 contribute to cellular differentiation processes, while TNFR1 and TNFR2 are involved in cell type-specific renal injury.
Description
Recombinant human TNFR2, expressed in E. coli, is a non-glycosylated polypeptide chain containing amino acids 23-206 of the TNFR2 protein. This 184-amino acid fragment has a molecular weight of 24.45 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag. TNFR2 is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
TNFR2 protein is supplied in a buffer consisting of 20 mM Tris-HCl (pH 8), 5 mM EDTA, and 50% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of TNFR2 is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Source
Escherichia Coli.
Amino Acid Sequence
LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWV
PECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSD
VVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT.

Product Science Overview

Introduction

Tumor Necrosis Factor Receptor Type 2 (TNFR2), also known as Tumor Necrosis Factor Receptor Superfamily Member 1B (TNFRSF1B) and CD120b, is one of the two primary receptors that bind to Tumor Necrosis Factor-alpha (TNFα). TNFR2 is a membrane receptor that plays a crucial role in various physiological and pathological processes, including immune response, inflammation, and tumor progression .

Structure and Function

TNFR2 consists of an extracellular region with four cysteine-rich domains that facilitate binding to TNFα. Unlike its counterpart, Tumor Necrosis Factor Receptor Type 1 (TNFR1), TNFR2 lacks a death domain (DD) in its intracellular structure, which results in different signaling pathways and functions when bound to TNFα .

Role in Tumor Microenvironment

TNFR2 is expressed in various tumor cells and certain immune cells, such as regulatory T cells (Tregs) and myeloid-derived suppressor cells (MDSCs). It contributes significantly to the tumor microenvironment by promoting tumor cell growth, activating immunosuppressive cells, and supporting immune escape . TNFR2’s activation mechanism involves recruiting a complex composed of adapter proteins, such as TNF receptor-associated factor 2 (TRAF2) and apoptosis-related markers like cIAP1/2 .

Therapeutic Potential

The dual role of TNFR2 in promoting both tumor progression and immune regulation makes it a promising target for cancer therapy. Antagonists and agonists targeting TNFR2 have shown significant anti-tumor activity in preclinical studies . These therapeutic agents can either inhibit the immunosuppressive functions of TNFR2 or enhance its ability to stimulate cytotoxic T-cells, thereby providing a multifaceted approach to cancer treatment .

Human Recombinant TNFR2 (His Tag)

Human recombinant TNFR2 with a His tag is a laboratory-produced version of the receptor, designed for research and therapeutic purposes. The His tag, a sequence of histidine residues, facilitates the purification and detection of the recombinant protein. This recombinant form is used in various studies to understand the receptor’s function, signaling pathways, and potential as a therapeutic target .

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