TNF a Rat, His

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag
Cat. No.
BT25369
Source
Escherichia Coli.
Synonyms
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by analysis 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.
Shipped with Ice Packs
In Stock

Description

TNF a Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235a.a.) and having a molecular mass of 19.9kDa.
TNF a is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tumor necrosis factor (TNF) is a cytokine that plays a key role in systemic inflammation. It belongs to a family of cytokines responsible for stimulating the acute phase reaction. Primarily secreted by macrophages, TNF exerts various effects, including apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis, and viral replication. It also participates in lipid metabolism and coagulation. TNF's principal function lies in regulating immune cells. Dysregulation and excessive production of TNF are implicated in numerous human diseases, such as autoimmune disorders, insulin resistance, and cancer.
Description
Recombinant Rat TNF alpha, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 181 amino acids (80-235 a.a.). It possesses a molecular mass of 19.9 kDa. This TNF alpha variant is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The TNF alpha protein solution (1 mg/ml) is supplied in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90.0% as determined by SDS-PAGE analysis.
Synonyms
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

Product Science Overview

Introduction

Tumor Necrosis Factor-alpha (TNF-α) is a multifunctional cytokine involved in various physiological and pathological processes. It plays a significant role in inflammation, immunity, apoptosis, and cell survival. The recombinant form of TNF-α, particularly the rat version with a His tag, is widely used in research to study its biological functions and therapeutic potential.

Structure and Expression

Recombinant Rat TNF-α with a His tag is typically expressed in HEK 293 cells, ensuring high purity and proper folding of the protein. The His tag facilitates purification and detection of the protein in various assays. The recombinant protein is often used in applications such as sELISA and SDS-PAGE .

Biological Functions

TNF-α is primarily secreted by macrophages and can induce cell death in certain tumor cell lines. It acts as a potent pyrogen, causing fever by directly stimulating interleukin-1 secretion. TNF-α is also implicated in the induction of cachexia, a wasting syndrome commonly seen in chronic diseases .

Under certain conditions, TNF-α can stimulate cell proliferation and induce cell differentiation. It plays a role in angiogenesis by inducing VEGF production synergistically with IL-1β and IL-6. Additionally, TNF-α induces insulin resistance in adipocytes by inhibiting insulin-induced IRS1 tyrosine phosphorylation and glucose uptake .

Signaling Pathways

TNF-α exerts its effects through two receptors: TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. The interaction with these receptors activates several signal transduction pathways, leading to diverse biological functions. The soluble form of TNF-α is derived from the membrane-bound form through proteolytic processing. The membrane-bound form is further processed by SPPL2A or SPPL2B, producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space .

Applications in Research

Recombinant Rat TNF-α with a His tag is used in various research applications, including:

  • sELISA: To quantify TNF-α levels in biological samples.
  • SDS-PAGE: To analyze the purity and molecular weight of the protein.
  • Cell Culture Studies: To investigate the effects of TNF-α on cell proliferation, differentiation, and apoptosis.
Therapeutic Potential

TNF-α has been explored for its therapeutic potential in cancer treatment. It has shown promise in the regional treatment of locally advanced soft tissue sarcomas and metastatic melanomas. TNF-α acts synergistically with cytostatic drugs, enhancing their efficacy by targeting tumor-associated vasculature and inducing hyperpermeability and destruction of the vascular lining .

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