Apoptosis, or programmed cell death, is a well-documented phenomenon in many cellular systems. (1) It plays a key role in tissue and organ development as well as in adult tissues during cell turnover. Apoptosis can be induced by a variety of internal and external stimuli including growth factor deprivation, cytokine treatment, antigen-receptor engagement, cell-cell interactions, irradiation and glucocorticoid treatment. (2) Bcl-2 and one of its homologues, Bcl-xL, protect cells from apoptosis (3,4), while other homologues of Bcl-2 such as Bax, Bad and Bak have been shown to enhance apoptosis. (5-8) Bcl-xL has been shown to block apoptosis which is induced by a variety of stimuli and, under certain conditions, offers greater protection against apoptosis than Bcl-2. (9-13) In contrast, Bad and Bax inhibit the protective functions of Bcl-xL and Bcl-2, respectively. Although heterodimerization between Bcl-xL/Bad and Bcl-2/Bax was originally thought to be essential for the differential anti-apoptotic activity of Bcl-xL and Bcl-2, (5,14) other results suggest that the formation of heterodimers may not be necessary for this death-repressing activity. (15,16) Mab 7B2.5 recognizes both human and rodent Bcl-xL. (17)
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
BAG3 - Hsp70 is my friend! The BAG proteins are a large family of chaperone regulators governing a wide range of cell processes such as proliferation, survival, stress response, tumorigenesis, neuronal differentiation, growth arrest and apoptosis as reviewed in Takayama et al1.... Read full blog post.
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