BCL2 Protein, Rat (Cell-Free, His)

The BCL2 protein is involved in suppressing apoptosis, or programmed cell death, in various cell systems, including factor-dependent lymphohematopoietic and neural cells. It regulates cell death by controlling the permeability of the mitochondrial membrane. BCL2 functions in a feedback loop system with caspases, inhibiting their activity by preventing the release of cytochrome c from the mitochondria and/or binding to the apoptosis-activating factor (APAF-1). Additionally, BCL2 acts as an inhibitor of autophagy, interacting with BECN1 and AMBRA1 to inhibit their autophagy function. It may also attenuate inflammation by impairing NLRP1-inflammasome activation, CASP1 activation, and IL1B release. BCL2 forms homodimers and heterodimers with BAX, BAD, BAK, and Bcl-X(L). Heterodimerization with BAX is necessary for its anti-apoptotic activity. BCL2 interacts with various proteins, including EI24, APAF1, BBC3, BCL2L1, BNIPL, MRPL41, TP53BP2, FKBP8, BAG1, RAF1, EGLN3, G0S2, RTL10/BOP, SCF(FBXO10) complex, NLRP1, GIMAP3/IAN4, GIMAP4/IAN1, GIMAP5/IAN5, BCAP31, IRF3, BECN1, and AMBRA1. These interactions have various effects on BCL2 activity, such as targeting it to the mitochondria or inhibiting its anti-apoptotic function.