Antibody catalog

Phosphatidylinositol 3-kinases (PI3Ks) are a group of lipid kinases with important roles in signal transduction. PI3Ks are involved in signal propagation for diverse receptors including tyrosine kinase receptors and G-protein coupled receptors. Class I PI3Ks consist of two subunits: the regulatory p85 subunit and the catalytic p110 subunit (1). p85 binds to phosphorylated tyrosine residues found on activated tyrosine kinase receptors and mediates the translocation of the p110 subunit to the cell membrane (2).

C/EBP homologous protein (CHOP) is a transcription factor that regulates apoptosis in response to cellular stress. CHOP also known as growth arrest and DNA damage 153 (GADD153) was first cloned because of its induction in response to genotoxic stress such as UV irradiation. CHOP has now been shown to be induced mainly by ER-stress (1). CHOP is normally expressed at low levels and localizes to the cytoplasm. Cellular stress triggers an upregulation of CHOP levels and accumulation in the nucleus where it can act as either a transcriptional repressor or activator (1).

T-cells infiltrating sites of inflammation of the skin typically express the cutaneous lymphocyte-associate antigen (CLA). This antigen is defined by the binding of the monoclonal CLA antibody HECA-452. The CLA antigen is a fucose-containing oligosaccharide and is found on many of the ligands that are recognized by the adhesion proteins P-selectin and E-selectin. CLA is primarily expressed by memory T-cells.

Cellular inhibitor of apoptosis protein-1 (cIAP-1) is an anti-apoptotic protein that is able to bind to caspases and inhibit their activity. Additionally cIAP-1 contains a RING domain with E3 ubiquitin ligase activity that is able to mediate the regulation of NF-kB signaling through the ubiquitination and degradation of various substrate proteins. Depending on cellular context, the RING domain of cIAP-1 can either promote or inhibit apoptosis.

Autophagy is a process by which cells degrade and recycle damaged organelles or misfolded proteins. These various cargo are engulfed in a double-membrane structure called the autophagosome. The autophagosome then fuses with the lysosome to facilitate the degradation of the cargo. This process requires the concerted effort of an extensive network of proteins. One of the early steps of autophagosome assembly is the formation of the large multimeric ATG12-ATG5-ATG16 complex.

Autophagy is an essential cellular process whereby damaged proteins and organelles are degraded and recycled. Autophagy, while happening constantly at a basal level, is tightly regulated and can be further induced under cellular stress. One of the regulators of the early steps of autophagy is ATG4. The ATG4 family of cysteine proteases consists of 4 homologs: ATG4A, ATG4B, ATG4C, and ATG4D.

The heat-shock protein 90 (HSP90) family is a group of highly conserved molecular chaperones with important functions in protein folding and in signal transduction. The HSP90 protein structure is so well conserved that some HSP90 antibodies are reactive with a broad range of species from humans to chickens (1). In humans there are 17 known genes encoding the HSP90 family members. The HSP90 family consists of 4 different classes: HSP90AA, HSP90AB, HSP90B, and TRAP.

The heat shock protein 70 (Hsp70) family are a group of chaperones involved in various cellular processes including protein folding and protein degradation. In addition to maintaining normal cellular homeostasis by processing newly synthesized protein, the Hsp70 family is also important in controlling intracellular signaling pathways by regulating the folding and activity of signaling proteins. The various groups within the Hsp70 family are characterized by their expression levels, activities, and subcellular localization (1).

Fms-like tyrosine kinase-3 (FLT3) is a Type III receptor tyrosine kinase expressed by hematopoietic progenitor cells. FLT3 is also sometimes referred to as FLK2 or CD135. The FLT3 protein exists in two states- membrane bound (160 kDa) and cytoplasmic (140 kDa) (1). The FLT3 ligand induces autophosphorylation of FLT3 which allows binding of scaffold and effector molecules. Activated FLT3 is capable of phosphorylating and activating PI3K, PLC-γ, Shc, Grb2, and Src (2). FLT3 signaling ultimately activates the AKT and MAPK pathways to promote cell growth and survival.

Akt1 is one of three isoforms of Akt belonging to the AGC family of serine/threonine kinases (Akt1, Akt2, and Akt3). All Akt isoforms contain an N-terminal Plekstrin Homology (PH) domain, a C-terminal regulatory domain, and a central catalytic kinase domain (1). Akt is a major downstream target of the PI3-K signaling pathway. The Akt1 isoform is fully activated by phosphorylation at three sites- T308, T450, and S473. Akt1 resides in an inactive state due to intramolecular interactions between the PH domain and the kinase domain.