tnf-α

TNF alpha Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 20.3 kDa and the accession number is P01375.

TNF alpha Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 20.3 kDa and the accession number is P01375.

TNF alpha Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 18.35 kDa and the accession number is P79337.

TNF alpha Protein, Rat, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.4 kDa and the accession number is P16599.

TNF alpha Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 45.8 kDa and the accession number is P01375.

TNF alpha Protein, Human, Recombinant, Biotinylated is expressed in E. coli expression system. The predicted molecular weight is 17.5 kDa and the accession number is P01375.

Tumor necrosis factor alpha (TNFα) is the prototypic ligand of the TNF superfamily. TNFα forms a homotrimer and functions by activating two types of receptors TNF-R1 (TNF receptor type 1,p55R) and TNF-R2 (TNF receptor type 2,p75R). TNFα is a pleiotropic cytokine that is capable to promote inflammation, to induce apoptotic cell death, and to inhibit tumorigenesis and viral replication. TNFα is a potent lymphoid factor that exerts cytotoxic effects on a wide range of tumor cells and certain other target cells.

TNF alpha Protein, Cynomolgus, Rhesus, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.4 kDa and the accession number is NP_001040614.1.

TNF alpha Protein, Human, Recombinant (aa 77-233, His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 16 KDa and the accession number is P01375.

TNF alpha Protein, Cynomolgus, Recombinant, Biotinylated is expressed in E. coli expression system. The predicted molecular weight is 17.4 kDa and the accession number is P79337.

TNF alpha Protein, Mouse, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.39 kDa and the accession number is P06804.

TNF alpha Protein, Ferret, Recombinant (His) is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 18.88 kDa and the accession number is A3FBF1.

TNF alpha Protein, Human, Recombinant (aa 57-233, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 18 KDa and the accession number is P01375.

TNF alpha Protein, Canine, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.3 kDa and the accession number is A9LMQ0.

TNF alpha Protein, Ferret, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.3 kDa and the accession number is A3FBF1.

TNF alpha Protein, Mouse, Recombinant, Biotinylated is expressed in E. coli expression system. The predicted molecular weight is 17.4 kDa and the accession number is P06804.

TNF alpha Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.5 kDa and the accession number is P01375.

TNF RII Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 60-90 KDa and the accession number is P20333.

TNF RII Protein, Human, Recombinant (mFc) is expressed in HEK293 mammalian cells with C-mFc tag. The predicted molecular weight is 60 KDa and the accession number is P20333.

Ephrin-A1 is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. Ephrin-A1 can be induced by TNF and IL1B. Its expression levels can be down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells. Soluble Ephrin-A1 is necessary for the transformation of HeLa and SK-BR3 cells and participates in the relocalization of EPHA2 away from sites of cell-cell contact during transformation. Ephrin-A1 plays an important role in angiogenesis and tumor neovascularization.

Lymphotoxin-alpha, also known as LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA TNFSF1, and TNFB, is a secreted protein that belongs to the tumor necrosis factor family. TNF-beta TNFSF1 Lymphotoxin alpha is highly inducible, secreted, and exists as a homotrimeric molecule. It is a cytokine that in its homotrimeric form binds to TNFRSF1A TNFR1, TNFRSF1B TNFBR, and TNFRSF14 HVEM. In its heterotrimeric form with LTB, TNF-beta TNFSF1 Lymphotoxin alpha binds to TNFRSF3 LTBR. Lymphotoxin is produced by lymphocytes and cytotoxic for a wide range of tumor cells. TNF-beta TNFSF1 Lymphotoxin alpha forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. It mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. TNF-beta TNFSF1 Lymphotoxin alpha is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis. Genetic variations in TNF-beta TNFSF1 Lymphotoxin alpha are a cause of susceptibility psoriatic arthritis which is an inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy.

Angiopoietin-like 7 (ANGPTL7) is a secreted glycoprotein that is structurally related to the angiopoietins. Members of this protein family contain an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL7 shares 89% aa sequence identity with mouse and rat ANGPTL7. It is secreted as a 45-50kDa monomer that forms disulfide-linked homotrimers and tetramers via the coiled coil domain. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Its production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-β and in cartilage by TNF-α. Overexpression of ANGPTL7 in trabecular meshwork cells inhibits the production of collagen and proteoglycans. When overexpressed in tumor cells it promotes collagen and proteoglycan deposition but inhibits tumor xenograft progression and tumor angiogenesis.

Amelotin (AMTN) is a tooth enamel protein which is expressed in maturation-stage ameloblasts and also in the internal basal lamina of junctional epithelium, a unique epithelial structure attached to the tooth surface which protects against the constant microbiological challenge to the periodontium. TNF-α stimulates AMTN gene transcription in human gingival epithelial cells via C EBP1, C EBP2, and YY1 elements in the human AMTN gene promoter.AMTN mRNA levels increased at 6 h and reached maximum at 24 h in GE1 cells. Luciferase activities of the mouse AMTN gene promoter constructs were induced by TGFβ1. AMTN mRNA levels were induced at the initiation of apoptosis by TGFβ1, which mediated through the Smad3 bindings to SBEs in the mouse AMTN gene promoter. Amelotin (Amtn) is a recently identified enamel protein secreted by ameloblasts at late stage of enamel development. Runt‑related transcription factor 2 (Runx2) in combination with the coactivator core‑binding factor β (Cbfβ) regulates the early stages of tooth development.

The eotaxin subfamily of CC chemokines consists of eotaxin-1 CCL11, eotaxin-2 CCL24 and eotaxin-3 CCL26. All eotaxins induce the trafficking of eosinophils to the sites of inflammation via CC chemokine receptor 3 (CCR3), which is also expressed by several different cell types, including basophils, dendritic cells, smooth muscle cells, epithelial cells and fibroblasts. The sequence similarity between the three eotaxins is limited (<4%), but their functional properties are very similar. Eotaxin-1 and -2 are expressed by both haematopoietic and non-haematopoietic cells, but eotaxin-3 expression has been reported to be limited to non-haematopoietic cells. Interleukin (IL)-4 is the main inducer for eotaxin-3 expression, whereas eotaxin-1 is up-regulated by IL-4 and the proinflammatory cytokine tumour necrosis factor (TNF)-α. Eotaxin-3 is expressed in vascular endothelial cells and human dermal fibroblasts after IL-4 and IL-13 stimulation, and this is dependent upon the IL-4- IL-13-specific transcription factor, signal transducers and activator of transcription (STAT)-6. Eotaxin-3 is expressed on the surface of IL-4-stimulated endothelial cells and promotes eosinophil transmigration.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Tumour necrosis factor alpha (TNF-α) is a pleiotropic cytokine with both injurious and protective functions, which are thought to diverge at the level of its two cell surface receptors, TNFR1 and TNFR2. In the setting of acute injury, selective inhibition of TNFR1 is predicted to attenuate the cell death and inflammation associated with TNF-α, while sparing or potentiating the protective effects of TNFR2 signalling.

Guanylate-binding protein 1 (GBP-1) is a member of the GBP family whose members are GTPases induced in response to interferon-λ (IFN-λ), with seven highly homologous members in humans, termed HuGBP-1 to HuGBP-7. GBP-1 expression is induced by type1 and type2 interferons, including IFN-λ and also by interleukin-1β (IL-1β), IL-1α, and tumor necrosis factor-α (TNF-α). GBP-1 is key to the protective immunity against microbial and viral pathogens. GBP-1 was only secreted from endothelial cells. Secretion occurred without the presence of a leader peptide. Secretion procession is a nonclassical, likely ABC transporter-dependent, pathway and independent of GBP-1 GTPase activity and isoprenylation, and did not require additional interferon-λ-induced factors. Clinically most important was the detection of significantly increased GBP-1 concentrations in the cerebrospinal fluid of patients with bacterial meningitis as compared to control patients.

B-cell activating factor (BAFF), also known as BLyS, TALL-1, THANK, and TNFSF13B, is a transmembrane glycoprotein in the TNF ligand superfamily. BAFF is a cytokine and serves as a ligand for receptors TNFRSF13B (TACI), TNFRSF17 (BCMA), and TNFRSF13C (BAFFR). BAFF can promotes the survival, proliferation and maturation of B lymphocytes, which are key elements in the pathogenesis of systemic lupus erythematosus (SLE). This cytokine is encoded on TNFSF13B gene, and diverse single-nucleotide polymorphisms have been associated with susceptibility in diferent autoimmune disorders. BAFF is a transmembranal protein expressed on myeloid lineage and some epithelial cells, through diferent stimuli such as IFN-γ, IFN-α, interleukin (IL)-10, Toll-like receptors (TLR)-3, TLR-4 and TLR-7.

Pre-B cell colony enhancing factor (PBEF) was originally identified as a cytokine that potentiated the clonal expansion and differentiation of pre-B cells, but it is also acknowledged to be the ubiquitous intracellular enzyme nicotinamide phosphoribosyltranferase (NAMPT) and the adipokine “visfatin”. PBEF is constitutively expressed in the fetal membranes where its greatest expression is in the amnion. It has intracellular and extracellular forms. Most of the intracellular functions of PBEF are due to its role as a Nampt which can induce angiogenesis through upregulation of VEGF and VEGFR and secretion of MCP-1. Extracellular PBEF has been shown to increase inflammatory cytokines, such as TNF-α, IL-1β, IL-16, and TGF-β1. PBEF also increases the production of IL-6, TNF-α, and IL-1β in CD14+ monocyctes, macrophages, and dendritic cells, enhances the effectiveness of T cells.

Ectodysplasin A receptor (EDAR) is a type I transmembrane protein of the TNF-α receptor superfamily which plays a key role in ectodermal differentiation. EDAR was encoded by the mouse downless gene and defective in human dominant and recessive forms of autosomal hypohidrotic ectodermal dysplasia (EDA) syndrome. The extracellular domain of EDAR contains 14 cysteine residues, six of which approximate the TNFRSF cysteine-rich region, the cytoplasmic domain contains a region with homology to the death domains found in other TNFRSF members. EDAR has been suggested to be an early and important promoter of placode development in all ectodermal organs, such as uch as hair follicles, teeth and sweat glands. EDA-A1, the A1 isoform of EDA, is the EDAR ligand. EDA and EDA are implicated in appendage development by the cloning of a gene underlying hypohidrotic ectodermal dysplasia (HED) in mouse and human. HED is characterized by agenesis or malformation of ectoderm-derived appendages, such as teeth, sweat glands and hair follicles, while the skin itself develops normally.

Surfactant Pulmonary-Associated Protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that places it in a subset of pattern recognition proteins termed defense collagens. SP-D is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures and induced in cardiac smooth muscle and endothelial cells. It binds both secreted and transmembrane proteins that transduce its function. It binds human neutrophil defensins, modulating influenza anti-viral defense. It binds MD-2 LY96, a secreted protein that cooperates with Toll-like receptors (TLRs) in the response of macrophages to bacterial lipopolysaccharides (LPS) or cell wall components. It also binds macrophage CD14 and TLRs directly, blocking binding of LPS and down-regulating TNF-α secretion. SP-D binding of both SIRPα and the calreticulin CD91 complex on macrophages allows for a graded response to environmental challenge.

ADAM17 is a member of the ADAM protein family of disintegrins and metalloproteases. ADAM17 is ubiquitously expressed in the human colon, with increased activity in the colonic mucosa of patients with ulcerative colitis, a main form of inflammatory bowel disease. The expression of ADAM17 may be inhibited by ethanol. It is involved in the processing of tumor necrosis factor alpha (TNF-α) at the surface of the cell, and from within the intracellular membranes of the trans-Golgi network. ADAM17 also plays a role in the release of a diverse variety of membrane-anchored cytokines, cell adhesion molecules, receptors, ligands, and enzymes. ADAM17 may play a prominent role in the Notch signaling pathway, during the proteolytic release of the Notch intracellular domain (from the Notch1 receptor) that occurs following ligand binding.