Recombinant humaan PELI2-eiwit

PELI2 is an E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. This protein is involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. It mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. PELI2 may be important for LPS- and IL1B-induced MAP3K7-dependent, but not MAP3K3-dependent, NF-kappa-B activation. It can activate the MAP (mitogen activated protein) kinase pathway leading to activation of ELK1. Recombinant human PELI2 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

E3 ubiquitin-protein ligase pellino homolog 2, PELI2 - pellino E3, Pellino-2

E.coli

Human

His-Tag

SDS-PAGE

0.5 mg/mL (determined by Bradford assay)

> 80% by SDS-PAGE

48.8 kDa (443aa) confirmed by MALDI-TOF

PELI2, E3 ubiquitin-protein ligase pellino homolog 2, PELI2-pellino E3, Pellino-2, ATGP2792-10 µg, ATGP2792-20 µg, ATGP2792-50 µg, ATGP2792-100 µg, ATGP2792-250 µg, ATGP2792-500 µg, ATGP2792-1 mg, ATGP2792-10, ATGP2792-20, ATGP2792-50, ATGP2792-100, ATGP2792-250, ATGP2792-500, ATGP2792-1

Jensen L.E., et al (2003) . FEBS Lett. 545:199-202; ; Strelow A., et al (2003) . FEBS Lett. 547:157-161

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 20% glycerol, 1mM DTT

Signal Transduction

NP_067078

Q9HAT8

Human

MFSPGQE EHCAPNKEPV KYGELVVLGY NGALPNGDRG RRKSRFALYK RPKANGVKPS TVHVISTPQA SKAISCKGQH SISYTLSRNQ TVVVEYTHDK DTDMFQVGRS TESPIDFVVT DTISGSQNTD EAQITQSTIS RFACRIVCDR NEPYTARIFA AGFDSSKNIF LGEKAAKWKN PDGHMDGLTT NGVLVMHPRG GFTEESQPGV WREISVCGDV YTLRETRSAQ QRGKLVESET NVLQDGSLID LCGATLLWRT ADGLFHTPTQ KHIEALRQEI NAARPQCPVG LNTLAFPSIN RKEVVEEKQP WAYLSCGHVH GYHNWGHRSD TEANERECPM CRTVGPYVPL WLGCEAGFYV DAGPPTHAFT PCGHVCSEKS AKYWSQIPLP HGTHAFHAAC PFCATQLVGE QNCIKLIFQG PID