Zitiert in 1 Publikation.
Der Maus Monoklonal anti-BCL2L1 Antikörper (Klon 7B2-5) (ABIN135021) detektiert spezifisch BCL2L1 in FACS.
Dieser Antikörper reagiert spezifisch mit Proben aus Human.
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
Probenmenge
1 mL
Beschränkungen
Nur für Forschungszwecke einsetzbar
Konzentration
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
Konservierungsmittel
Without preservative
Handhabung
Each reagent is stable for the period shown on the bottle label if stored as directed.
Lagerung
4 °C
Informationen zur Lagerung
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))
Andere Bezeichnung
Bcl-xL
Hintergrund
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.