Beclin-1 Complex Antibody Sampler Kit #59187
Product Information
Kit Usage Information
Protocols
Product Description
The Beclin-1 Complex Antibody Sampler Kit provides an economical means of detecting proteins that are part of the Beclin-1 complexes. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.
Specificity / Sensitivity
Each antibody in the Beclin-1 Complex Antibody Sampler Kit detects endogenous levels of its target protein. Rubicon (D9F7) Rabbit mAb detects a band of unknown origin at 55 kDa.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Thr72 of human Beclin-1, Lys630 of human PI3 Kinase Class III, Arg70 of human Atg14, Gly502 of human UVRAG, and Leu210 of human Rubicon. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly825 of human PIK3R4 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
A number of studies have identified distinct complexes involving Beclin-1 and PI3K Kinase Class III with specific roles in autophagy and vesicle trafficking (1,2). These complexes commonly contain Beclin-1, PI3KC3/VSP34, and PIK3R4/VPS15 and function to catalyze the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate. Specificity of PI3KC3 activity is regulated by additional binding partners. Complex 1 contains Atg14 which is required for early stages of autophagosome nucleation (3,4). Complex 2 lacks Atg14, but instead contains UVRAG, and is important for autophagosome maturation and endocytic trafficking (4-6). A third complex, containing both UVRAG and Rubicon, negatively regulates canonical autophagy (7,8). Importantly, this complex containing Rubicon is critical for a related process of LC3-associated phagocytosis (LAP) in which extracellular pathogens binding to cell surface receptors are engulfed by a single membrane phagosome and degraded by the lysosome (9,10).
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- Heckmann, B.L. and Green, D.R. (2019) J Cell Sci 132(5). pii: jcs222984. doi: 10.1242/jcs.222984.
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