Antibodies

Integrins are a large family of trasmembrane proteins involved in cell adhesion and form a link between the intracellular cyskeletal proteins and extracellular matrix proteins. Integrins exist as heterodimers consisting of alpha and beta subunits. In addition to cell adhesion these integrin complexes play key roles in diverse processes such as signal transduction, cell migration, proliferation, differentiation, and apoptosis. Integrins consist of three domains: the extracellular domain, the transmembrane domain, and the cytoplasmic tail.

Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is an abundant ubiquitously expressed protein with important roles in the regulation of gene expression. hnRNP A1 is involved in transcription as well as the splicing, trafficking, and translation of RNA transcripts. hnRNP A1 binds RNA targets in a sequence specific manner through two N-terminal RNA recognition motifs (RRM) and a C-terminal RGG box RNA binding domain.

B-cell lymphoma 2 (Bcl-2) protein is an oncogene that normally acts as an apoptotic inhibitor and localizes to the mitochondrial membrane where it prevents the release of cytochrome c. The Bcl-2 protein family consists of over 20 proteins each containing at least one Bcl-2 homology (BH) domains and have either proapoptic or antiapoptotic activities.

Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric transcription factor consisting of alpha and beta subunits. The levels of functional HIF-1 in the cell depends on the level of oxygen allowing cells to respond to hypoxic conditions. HIF-1α is a ubiquitously expressed protein containing an oxygen-dependent degradation domain that under normal conditions regulates its constant degradation. HIF-1 beta, on the other hand, is a stable constitutively expressed protein that localizes to the nucleus.

Atg9 is the only essential transmembrane protein involved in cellular autophagy. Autophagy regulates cellular homeostasis by allowing the turnover and recycling of misfolded proteins and damaged organelles. Formation of the double-membrane isolation membrane that forms the pre-autophagosome requires the contribution of highly mobile cytoplasmic vesicles containing Atg9. These vesicles are derived from recycling endosomes and are responsible for recruiting and delivering lipid components to the assembling autophagosome.

Microtubule-associated protein-1 light chain 3 (LC3/LC3B) is a ubiquitin-like protein involved in the formation of the autophagosome. It is homologous to the yeast Atg8 protein. Autophagosomes are important for the degradation and recycling of intracellular cargo such as misfolded proteins or damaged organelles. Upon induction of autophagy, LC3 is conjugated to the lipid phosphatidylethanolamine (PE) by the Atg12-Atg5-Atg16 protein complex.

Hypoxia-inducible factor 1 (HIF-1) allows cells to respond to changing levels of oxygen in the environment. HIF-1 is a heterodimeric transcription factor consisting of alpha and beta subunits. Under normal conditions HIF-1 alpha is continuously synthesized and degraded. HIF-1 alpha degradation is mediated through an oxygen-dependent degradation domain that is hydroxylated and leads to ubiquitylation and proteolysis. HIF-1 beta on the other hand is constitutively expressed and localizes to the nucleus.

Survivin is an anti-apoptotic protein which is the smallest protein within a large family of proteins including X-linked IAP, c-IAP1 and 2, IAP-like protein-2, melanoma IAP, NAIP, and Livin. Survivin is responsible for a wide range of basic cellular functions that include the cell cycle regulation, fetal development, cell migration, and tumor progression.

Fanconi anemia (FANC) is a rare, autosomal-recessive genetic disorder that is a heterogeneous cancer susceptibility condition that manifests with a wide range of symptoms such as congenital malformations, deteriorating bone marrow failure, DNA-damage hypersensitivity, genomic instability, and increased cancer incidence. FANCD2 is a component within the protein complex that is involved in a cell's resistance to DNA cross-linking and subsequent DNA synthesis arrest that is stimulated by the insult of ionizing radiation (IR).

The Beclin 1 protein is a central regulator of autophagy in mammalian cells. Autophagy is an essential process used to maintain cellular homeostasis by degrading and recycling cellular components such as damaged or worn out organelles and macromolecules. Autophagy is also activated in response to cellular stresses such as nutrient starvation or intracellular pathogens and can protect the cell from programmed cell death.