15 products were found matching "F0019-53M1.100"!

FADD was originally isolated as a protein that bound to the cytoplasmic domain of Fas in the yeast two-hybrid system. Sequence analysis revealed a region homologous to the death domain of Fas and TNFR-1. Subsequent biochemical studies have shown that FADD associates with Fas through interaction of the death domains....

Fas-associated death domain (FADD or Mort 1) functions as an important adaptor in coupling death signaling from membrane receptors, such as the Fas ligand and TNF family (DR3, DR4 and DR5), to caspase- 8 (1,2). FADD has a C-terminal death domain interacting with the cytoplasmic tail of the membrane receptor and an...

The susceptibility of primary splenic B cells to Fas-mediated apoptosis is regulated in a receptor-specific fashion (reviewed in 1). Terminal effectors of B cell Fas-resistance include the known anti-apoptotic proteins Bcl-xL, FLIP, and a recently identified protein termed FAIM (2). This molecule is broadly...

FAIM (Fas apoptosis inhibitory molecule) was identified as a protein that was inducibly expressed in B lymphocytes resistant to Fas-mediated apoptosis (1). Expression of FAIM inhibits receptor-mediated apoptosis in B cells as well as other cell types (1-3). FAIM is expressed in germinal center B cells, is positively...

CD95, also known as Fas and Apo-1, is a 40-50kD type I transmembrane glycoprotein and a member of the tumor necrosis factor receptor superfamily. It is expressed by activated lymphocytes, monocytes, neutrophils, fibroblasts and cell lines. Fas ligand binding to CD95 induces apoptosis in activated mature lymphocytes...

CD95, also known as Fas and Apo-1, is a 40-50kD type I transmembrane glycoprotein and a member of the tumor necrosis factor receptor superfamily. It is expressed by activated lymphocytes, monocytes, neutrophils, fibroblasts and cell lines. Fas ligand binding to CD95 induces apoptosis in activated mature lymphocytes...

Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Applications:...

Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. Applications: Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications not tested. Recommended Dilution: ELISA: 1:32,000, Western Blot: 0.5-1ug/ml, observed in human...

The human Fatty Acid Binding Protein is derived from the human FABP3 gene. FABPs are small intracellular proteins (~13-14kD) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of...

Fas-associated death domain (FADD or Mort 1) functions as an important adaptor in coupling death signaling from membrane receptors, such as the Fas ligand and TNF family (DR3, DR4 and DR5), to caspase- 8 (1,2). FADD has a C-terminal death domain interacting with the cytoplasmic tail of the membrane receptor and an...

Fas-associated death domain (FADD, also known as MORT1) is an important apoptosis adapter molecule involved in the Fas-mediated cell death pathway. FADD associates with the intracellular domain of FAS (CD95/APO-1) through their respective C-terminal death domains (DD). The N-terminal region of FADD contains a death...

Fas-associated death domain (FADD, also known as MORT1) is an important apoptosis adapter molecule involved in the Fas-mediated cell death pathway. FADD associates with the intracellular domain of FAS (CD95/APO-1) through their respective C-terminal death domains (DD). The N-terminal region of FADD contains a death...