protein

Fas/CD95 Protein, Human (HEK293)

HY-P7168

10 μg;50 μg

107;300 USD

Fas/CD95 Protein, Human (HEK293)

proteins

HEK293

10 μg;50 μg

107;300 USD

377622304

Fas receptor is a cell surface death receptor, can bind to Fas ligand to form death-inducing signaling complexes, such as Fas associated death domain proteins (FADD) [1] [2] . Fas receptor participates in the caspase cascade and regulate the activation of JNK and p38-K downstream. It is also involved in the signaling cascade of ERK/JNK MAPKs, activating MAPK3/ERK1, MAPK8/JNK and NF-κB, which has been implicated in the pathogenesis of various malignant tumors and immune system diseases [3] [4] . Human Fas receptor contain a death domain (230-314 a.a.) that plays a key role in regulating programmed death. Fas/CD95 Protein, Human (HEK293) has a full length of 157 amino acids (Q26-S172), produced in HEK293 cells with tag free.

Human

Fas receptor is the receptor for TNFSF6/FASLG, also known as apoptosis-mediating surface antigen FAS and Apo-1 antigen. It is a cell-surface protein that mediates apoptosis upon ligation with Fas ligand. Fas receptor belongs to tumor necrosis factor receptor superfamily, there are 7 isoforms produced by alternative splicing, some of which are candidates for nonsense-mediated mRNA decay (NMD). The Fas gene is expressed in several tissues in human and mouse, including thymus, spleen, ovary and heart, and on a number of cell types, including activated T- and B-lymphocytes. Isoform 1 and isoform 6 are expressed at equal levels in resting peripheral blood mononuclear cells. After activation there is an increase in isoform 1 and decrease in the levels of isoform 6 [1] . Fas receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. It interacts with its ligand to allow the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10 [2] . To be specific, the autoproteolytic processing of the caspase in the complex triggers a downstream caspase cascade, including activation of the acidic sphingomyelinase, consumption of sphingomyelin, release of ceramide, and subsequent activation of JNK and p38-K. Thus, Fas receptor acts fucntion via caspase’s regulation and leads to apoptosis [3] . Moreover, the signaling initiated from Fas is mediated by mitogen activated protein kinases (MAPKs) including extracellular-signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) which induce subsequent activation of NF-κB. Meanwhile, stimulation of Fas induced the expression of pro-inflammatory mediators such as matrix metalloproteinase (MMP)-9 and IL-8 [4] . The amino acid sequence of human Fas protein has low homology with that of rat and mouse, and the similarity rate is 49.54% and 48.93%, respectively.

rHuFASR/TNFRSF6; Tumor necrosis factor receptor superfamily member 6; Fas receptor; CD95; APT1; FAS1; Apo-1

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against PBS.

Room temperature in continental US; may vary elsewhere.