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.
Tumornecrosisfactor 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.
Pentraxin-related protein PTX3, also known as Tumornecrosisfactor-inducible gene 14 protein (TSG-14), belongs to the pentraxin family. PTX3 plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. It’s subunit is a disulfide-linked homooctamer that binds to C1q. PTX3 concentration is elevated in the joint fluid of patients with rheumatoid arthritis (RA), indicating that PTX3 may be a potential mediator of immune response. PTX3 may also function in the regulation of the uptake and clearance of apoptotic cells by dendritic cells. An in vivo study showed that PTX3 transgenic mice are more resistant to sepsis and endotoxemia compared to wild-type during inflammatory injury.
TROY Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 17 kDa and the accession number is Q9JLL3-1.
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.
Tumornecrosisfactor (TNF)-alpha-induced protein 8 (TNFAIP8) family is a newly identified protein with vital roles in maintaining immune homeostasis. Tumornecrosisfactor-alpha-inducible protein 8 (TNFAIP8) is a TNF-alpha inducible anti-apoptotic protein with multiple roles in tumor growth and survival. by the creation of cellular autophagy events, TNFAIP8 promotes cell survival and drug resistance in prostate cancer cells. TNFAIP8 regulates Hippo pathway through interacting with LATS1 to promote cell proliferation and invasion in lung cancer. TNFAIP8 may serve as a candidate biomarker for poor prognosis and a target for new therapies.
TROY Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with mFc tag. The predicted molecular weight is 41.95 kDa and the accession number is Q9JLL3-1.
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.
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.
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.
TROY Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 16.9 kDa and the accession number is Q9NS68-2.
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 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.
TROY Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 42.5 kDa and the accession number is Q9NS68-2.
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.
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.
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 tumornecrosisfactor-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.
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 tumornecrosisfactor 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.
Fractalkine(CX3CL1) is a single-pass type I membrane protein and belongs to the intercrine delta family. It consists of an extracellular NH2-terminal domain, a mucin-like stalk, a transmembrane α helix, and a short cytoplasmic tail. CX3CL1 exists in two forms: as a membrane-anchored or as a shed 80-95K glycoprotein. Soluble CX3CL1 is generated by limited proteolysis on the cell surface, and a disintegrin and metallopeptidase 10 (ADAM10) and ADAM17 tumornecrosisfactor-α-converting enzyme (ADAM17 TACE) participate in this shedding. It has been suggested that ADAM10 acts in the constitutive shedding, and ADAM17 acts in response to cell activation. The protein may play a role in regulating leukocyte adhesion and migration processes at the endothelium.