Human TNF alpha Protein 4518

$225.00 – $750.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Val77-Leu233

SKU: 4518parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P01375
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Tumor necrosis factor alpha (TNF-alpha), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism.Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation.
molecular weight	The protein has a predicted MW of 20.3 kDa. Due to glycosylation, the protein migrates to 21-25 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human TNF alpha Protein 4518

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Tumor necrosis factor alpha (TNF-alpha), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism.Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation.
Protein names Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
Gene names TNF,TNF TNFA TNFSF2
Protein family Tumor necrosis factor family
Mass 25644Da
Function Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Up-regulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:22517918, PubMed:16829952, PubMed:23396208). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (PubMed:12794819). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity).; The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.
Subellular location Cell membrane ; Single-pass type II membrane protein .; [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein.; [Tumor necrosis factor, soluble form]: Secreted .; [C-domain 1]: Secreted.; [C-domain 2]: Secreted.
Structure Homotrimer. Interacts with SPPL2B.
Post-translational modification The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis 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.; The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.; O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.; [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated at Lys-19 and Lys-20 by SIRT6, promoting its secretion.
Domain TOPO_DOM 1
Target Relevance information above includes information from UniProt accession: P01375
The UniProt Consortium

Data

Human TNF alpha, His Tag captured on CM5 Chip via anti-his antibody can bind Human TNFR2, mFc Tag with an affinity constant of 1.62 nM as determined in SPR assay (Biacore T200).

Immobilized Human TNF alpha, His Tag at 5µg/ml (100µl/Well) on the plate. Dose response curve for Human TNFR2, mFc Tag with the EC50 of 45.8ng/ml determined by ELISA (QC Test).

The purity of Human TNF alpha is greater than 95% as determined by SEC-HPLC.

Human TNF alpha on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.