Autophagy

ATG5 is a member of the ATG family that regulates autophagy, the evolutionary conserved homeostatic response to a diverse variety of self- and foreign-originating cellular stresses. ATG5 is ubiquitously expressed in cells and found co-localized with cytoplasmic non-muscle actin under normal resting conditions, but upon the triggering of apoptosis, ATG5 expression dramatically ramps up, and ATG5 directly conjugates with other related ATG family proteins to form autophagosomes.

Beclin 1 is the first mammalian gene identified as a mediator of autophagy, and plays important roles in development, tumorigenesis, and neurodegeneration.

PINK1 is a protein serine/threonine kinase (PTK) that protects the organelles from cellular stress and controls selective autophagy to clear damage. Exner, et. al. were among the first to report that PINK1 deficiency in humans was linked to autosomal recessive occurrences of Parkinson's disease (PD) and neurogenerative pathology (1).

LC3 is distributed ubiquitously in eukaryotes and is a heavily studied autophagy biomarker that was originally identified as a subunit of MAP1A and MAP1B. Because autophagy is a crucial process for maintaining normal neural networks and function, understanding neuronal autophagy is important. Young's group at Univ.

LC3B is subunit component of the LC3 autophagy biomarker associated with microtubule-associated proteins MAP1A and MAP1B and one of the best characterized markers to date. In resting state, it is cytosolic, but upon activation, is lapidated and becomes embedded in the autophagosomal membrane.

Autophagy is a conserved mechanism whereby cells form double membrane autophagosomes to sequester cytoplasmic components for subsequent destruction by fusion with lysosomes (eukaryotes) or vacuoles (yeast). Targets of autophagy include aging proteins, damaged organelles and invasive pathogens, and the resulting breakdown products can be recycled back to the cytoplasm for re-use under conditions of starvation (1).

LC3B, also known as microtubule-associated protein 1 light chain 3 beta (MAP1LC3B), is an autophagy gene that contributes appreciably to protein degradation. Autophagy is a highly synchronized and dynamic catabolic degradation activity that plays an essential role in cellular maintenance, development, antigen presentation and cell death.

Beclin 1 is the mammalian orthologue of the yeast Apg6/Vps30 gene. Beclin 1 can complement the defect in autophagy present in apg6 yeast strains and stimulate autophagy when overexpressed in mammalian cells (1) and can bind to Bcl2, an important regulator of apoptosis (2) suggesting a role in two fundamentally important cellular pathways: autophagy and apoptosis.

Microtubule-associated protein light chain 3 (LC3) is considered one of the definitive markers of autophagy, and its use is widespread in labs throughout the world. Despite its popularity, there are several considerations when employing LC3 antibodies in immunoassays, Western blots in particular.

MAP1LC3 (shortened to LC3 in our antibody catalog) is one of four mammalian homologues of autophagy-related protein 8 (Atg8). It has been identified as a light chain subunit of the microtubule-associated proteins MAP1A/MAP1B. A modified form of LC3, LC3-II, has been identified as a marker for the autophagosomal membrane in mammals.