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  • 产品名称：TumorNecrosisFactorReceptorSuperfamily,Member12A(TNFRSF12A)(AA28-79)(Active)pro

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  • 产品厂商：ACROBiosystems
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简单介绍：
TumorNecrosisFactorReceptorSuperfamily,Member12A(TNFRSF12A)(AA28-79)(Active)protein(FcTag)
详情介绍：
Characteristics This protein carries a human IgG1 Fc tag at the N-terminus. The protein has a calculated MW of 33 kDa. As a result of glycosylation, the protein migrates as 32-40 kDa under reducing (R) condition, and 65-80 kDa under non-reducing (NR) condition (SDS-PAGE).
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to bind CD155 in a functional ELISA.
Background Tumor necrosis factor receptor superfamily member 12A (TNFRSF12A) is also known as Fibroblast growth factor-inducible immediate-early response protein 14 (FN14 or FGF-inducible 14), Tweak-receptor, CD antigen CD266. TNFRSF12A contains one TNFR-Cys repeat. TNFRSF12A is highly expressed in heart, placenta and kidney. TNFRSF12A is receptor for TNFSF12/TWEAK, and is weak inducer of apoptosis in some cell types. TNFRSF12A / FN14 promotes angiogenesis and the proliferation of endothelial cells.
Molecular Weight 33 kDa
UniProt Q9NP84
Pathways Apoptosis, Regulation of Cell Size
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Tumor Necrosis Factor Receptor Superfamily, Member 12A (TNFRSF12A) (AA 28-79) (Active) protein (Fc Tag) (ABIN2181851) Human TWEAK R, Fc Tag on SDS-PAGE under reducing (R) and no-reducing (NR) conditions....
Background publications He, Dang, Saito, Watanabe, Kobayashi, Güntert, Kigawa, Tanaka, Muto, Yokoyama: "Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily." in: Protein science : a publication of the Protein Society, Vol. 18, Issue 3, pp. 650-6, 2009 (PubMed).

Wiley, Cassiano, Lofton, Davis-Smith, Winkles, Lindner, Liu, Daniel, Smith, Fanslow: "A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis." in: Immunity, Vol. 15, Issue 5, pp. 837-46, 2001 (PubMed).