tnf α

Expression system: E. coli
Length: 77-233, Partial
Activity: Cell Activity

Expression system: E. coli
Length: 57-233, Extracellular Domain
Activity: BLI、Cells

Expression system: E. coli
Length: 78-235, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 77-233, Partial
Activity: ELISA、SPR

Expression system: HEK293 Cells
Length: 77-233, Partial
Activity: ELISA、SPR

Expression system: HEK293 Cells
Length: 77-233, Partial
Activity: ELISA

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.

Expression system: HEK293 Cells
Length: 35-205, Full Length of Mature Protein
Activity: ELISA

Expression system: E. coli
Length: 18-277, Full Length of Mature Protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 18-277, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 34-202, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 59-234, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 134-285, Soluble Form
Activity: ELISA

Expression system: HEK293 Cells
Length: 23-257, Partial
Activity: BLI、ELISA、Cells

Expression system: HEK293 Cells
Length: 24-206, Partial
Activity: BLI、ELISA

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.

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.

Expression system: HEK293 Cells
Length: 27-346, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-491, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 27-189, Partial
Activity: Not Tested

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.

Expression system: E. coli
Length: 77-233, Partial
Activity: SPR、Cells

Expression system: E. coli
Length: 80-235, soluble form
Activity: Cell Activity

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.