Suggested positive control: 3T3 whole cell lysate, HeLa or NIH-3T3, antigen standard for TRAF3 (transient overexpression lysate).
Tumor necrosis factor (TNF) induced signaling is mediated through association of TNF receptor (TNFR) with adaptor proteins, such as TNF receptor associated proteins (TRAFs). TRAFs form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily (e.g. RANK, CD30, CD40, etc.) and the interleukin-1 receptor. The carboxy-terminal region of TRAFs is required for self-association and interaction with receptor cytoplasmic domains following ligand-induced oligomerization. Recent molecular cloning studies have lead to identification of six TRAFs (TRAF1-TRAF6). TRAF3, originally named CRAF1, interacts directly with the CD40 cytoplasmic tail through a region of similarity to the tumor necrosis factor-alpha (TNF-alpha) receptor-associated factors. TRAF3 binds only a single site, which contains the sequence PEQET, whereas TRAF1 and TRAF2 are capable of binding to either the PEQET site or an additional downstream domain.
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Protein Aliases: CAP-1; CD40 associated protein 1; CD40 binding protein; CD40 receptor associated factor 1; CD40 receptor-associated factor 1; CD40-binding protein; CD40BP; CRAF1; LAP1; LMP1-associated protein 1; RING-type E3 ubiquitin transferase TRAF3; TNF receptor-associated factor 3; TRAFAMN
Gene Aliases: AI528849; amn; CAP-1; CAP1; CD40bp; CRAF1; IIAE5; LAP1; T-BAM; TRAF3; Trafamn
Molecular Function: signaling molecule