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The protein encoded by FAIM protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. Additionally we are shipping FAIM Antibodies (104) and FAIM Proteins (9) and many more products for this protein.
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the anti-apoptotic effect of SRT1720 was mitigated by FAIM knockdown with a small interfering RNA-targeted FAIM. These results indicated that pretreatment with SRT1720 improves survival of aged hMSCs, and enhances their therapeutic efficacy for rat myocardial infarction (MI).
subcellular fractionation experiments revealed that, in contrast to FAIM-S and FAIM-L, FAIM-S_2a and FAIM-L_2a are able to localize to the nucleus, where they may have additional functions. In summary, here we report on two novel FAIM isoforms that may have relevant roles in the physiology and pathology of the nervous system
Data indicate that FAIM is a novel regulator of insulin signalling and plays an essential role in energy homoeostasis.
FAIM modulates IGF-1-induced Akt activation and IRF4 expression and has a role in multiple myeloma cell survival
FAIM (1-90) was crystallized and diffracted to a resolution of 2.5 A; the crystal belonged to space group P3(1), with unit-cell parameters a=b=58.02, c=71.11 A, alpha=beta=90, gamma=120 degrees.
Human keratinocytes were transfected with either Flip, Faim, or Lifeguard (LFG). Our results suggest that heterotopic expression of antiapoptotic proteins can induce the resistance of keratinocytes to a major mechanism of rejection.
Expression of the long form of Fas apoptotic inhibitory molecule (FAIML) results in the protection of neurons from the cytotoxic actions of death ligands.
FAIM acts to specifically enhance CD40 signaling for NF-kappaB activation, IRF-4 expression, and BCL-6 down-regulation in vitro, but has no effect on its own
The neuron-specific form of FAIM protein (FAIM-L) is a death receptor antagonist that stabilizes XIAP protein levels, thus preventing death receptor-induced neuronal apoptosis. Here we show that FAIM-L modulates synaptic transmission, prevents chemical-LTD induction in hippocampal neurons, and thwarts axon degeneration after nerve growth factor (NGF) withdrawal.
defined a TCR-induced FAIM/Akt/Nur77 signaling axis that is critical for modulating the apoptosis of developing thymocytes
The NMR solution structure of the C-terminal domain of murine FAIM is solved in isolation and revealed to be a novel protein fold, a noninterleaved seven-stranded beta-sandwich.
FAIM plays a novel role in modulating Fas-mediated apoptosis and acts through influencing the expression of c-FLIP and regulating the physical binding of caspase-8 to Fas.
FAIM is expressed in germinal center B cells, enhances interferon regulatory factor (IRF)4 expression, and is in turn positively regulated through IRF4 in a positive reinforcing (i.e., feed-forward) system.
The protein encoded by this gene protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. Several transcript variants encoding different isoforms have been found for this gene.
fas apoptotic inhibitory molecule 1
, Fas apoptotic inhibitory molecule
, Fas apoptosis inhibitory molecule 1
, uncharacterized protein LOC436668