BNIPL (BCL2/adenovirus E1B 19kD interacting protein like) is a novel proapoptotic protein belonging to the BNIPL family. It consists of a BNIP-2 and Cdc42GAP homology (BCH) domain. It is expressed in human placenta and lungs.
Immunogen
BNIPL (AAH74779.3, 1 a.a. ~ 275 a.a) full-length human protein.
BNIPL (BCL2/adenovirus E1B 19kD interacting protein like) is highly involved in the apoptotic pathways. The BCH domain of BNIPL performs in two critical pathways related to cell death. During DNA fragmentation, it directly interacts with the Bcl-2 as a linker protein. BNIPL also interacts with Cdc42GAP to stabilize the structural changes of chromosome during apoptosis. It has been reported that BNIPL may participate in the regulation of DNA fragmentation and membrane bleb formation pathways in apoptotic cells. BNIPL also plays a crucial role in the cell proliferation by binding to cell proliferation-related proteins, MIF (macrophage migration inhibitory factor) and GFER (growth factor erv1 (Saccharomyces cerevisiae-like).
World journal of gastroenterology, 10(9), 1286-1291 (2004-04-28)
Bcl-2/adenovirus E1B 19 ku interacting protein 2-like (BNIPL-2) is a novel protein recently identified in our laboratory. BNIPL-2 is homologous to human BNIP-2, a potentially proapoptotic protein, and can interact with Bcl-2 and Cdc42GAP and promote apoptosis in BEL-7402 cells.
Bcl-2/adenovirus E1B 19 kDa interacting protein 2-like, BNIP-2-like (BNIPL) is a recently cloned and characterized apoptosis-associated protein that shares 72% homology with BNIP-2. It is highly expressed in human placenta and lung. A yeast two-hybrid system was used to obtain
Biochemical and biophysical research communications, 308(2), 379-385 (2003-08-07)
The execution phase of apoptosis is characterized by marked changes in cell morphology that include contraction and membrane blebbing. Little is known about the mechanisms underlying this process. We report here the identification of a novel member of BNIPL family
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