Cited in 1 publication.
The Mouse Monoclonal anti-BCL2L1 antibody (Clone 7B2-5) (ABIN135021) specifically detects BCL2L1 in FACS.
The antibody is reactive with Human samples.
Applications: FC - Quality tested , IHC-PS - Reported in literature , ICC - Reported in literature , WB - Reported in literature , IP - Reported in literature , ELISA - Reported in literature
Working Dilutions: Flow Cytometry FITC and BIOT conjugates 3 g/106 cells PE conjugate 0.3 g/106 cells For flow cytometry, the suggested use of these reagents is in a final volume of 100 L Immunoblotting Purified (UNLB) antibody 1 g/mL
Sample Volume
1 mL
Restrictions
For Research Use only
Concentration
0.1 mg/mL
Buffer
0.1 mg of purified immunoglobulin in 1.0 mL of borate buffered saline, pH 8.2. No preservatives or amine-containing buffer salts added
Preservative
Without preservative
Handling Advice
Each reagent is stable for the period shown on the bottle label if stored as directed.
Storage
4 °C
Storage Comment
Store at 2-8°C
Gottschalk, Boise, Oltvai, Accavitti, Korsmeyer, Quintáns, Thompson: "The ability of Bcl-x(L) and Bcl-2 to prevent apoptosis can be differentially regulated." in: Cell death and differentiation, Vol. 3, Issue 1, pp. 113-8, (2006) (PubMed).
Target
BCL2L1
(BCL2-Like 1 (BCL2L1))
Alternative Name
Bcl-xL
Background
Apoptosis, or programmed cell death, is a well-documented phenomenon in many cellular systems. 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. Bcl-2 and one of its homologues, Bcl-xL, protect cells from apoptosis, while other homologues of Bcl-2 such as Bax, Bad and Bak have been shown to enhance apoptosis. 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. 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, other results suggest that the formation of heterodimers may not be necessary for this death-repressing activity.