Antibody catalog

Caspases are a family of cysteine-aspartic acid proteases that cleave caspase proenzymes as well as other protein substrates. Caspases are well known for their role in apoptosis, but they also play a significant role in other cellular processes including inflammation (1). Apoptotic caspases include Caspases-3, -6, -7, -8, and -9. Meanwhile, human inflammatory caspases include Caspases-1, -4, -5, and -12.

TSC2 is a tumor suppressor gene that encodes a 200 kDa protein called tuberin. TSC2 heterodimerizes with TSC1 to form a complex with GTPase-activating protein (GAP) activity. The C-terminus of TSC2 contains the GAP domain responsible for this catalytic activity. The complex was first discovered through its role in the tumor-forming condition Tuberous Sclerosis. Mutations in TSC1 and TSC2 can either destabilize the complex or compromise the GAP activity. The TSC1-TSC2 complex acts as a GAP for the small G-protein Rheb, expressed ubiquitously throughout the body (1).

Autophagy can be broken down into 4 main stages: phagophore nucleation, autophagosome elongation, autophagosome docking and fusion with a lysosome, and vesicle breakdown and degradation. ATG4B is one of four ATG4 homologs (ATG4A, ATG4B, ATG4C, and ATG4D) involved in autophagosome elongation. ATG4B encodes a 48 kDa protein called autophagin-1 that is a member of the C54 family of cysteine proteases.

TSC1 is a tumor suppressor gene that encodes a 130 kDa protein called hamartin. TSC1 was first identified as an oncogenic driver of Tuberous Sclerosis, a condition characterized by numerous benign tumors of the skin, brain, heart, and lungs. A mutation in TSC1 is responsible for the uncontrolled growth characteristic of these tumors. This discovery led to a greater understanding of the physiologic role of TSC1 as a negative cell cycle regulator. The distinct but related gene TSC2 encodes a 200 kDa protein called tuberin.

Human hepatocytes express important transport proteins that are responsible for the uptake and removal of organic anions from the blood. These proteins are members of the organic anion-transporting polypeptide (OATP) family and are essential for proper liver function. OATPs are encoded by the SLC21 gene family and contain 12 transmembrane alpha-helices and are primarily expressed in the liver. The OATP family transports endogenous substrates like bile salts and steroid hormones as well as exogenous molecules like anticancer drugs and imaging agents.

Thrombomodulin, also known as BDCA-3, is a glycosylated transmembrane protein present on the surface of vascular endothelial cells. Thrombomodulin is a high-affinity receptor for thrombin, a key protein in the coagulation cascade. Formation of the thrombomodulin-thrombin complex blocks the thrombin dependent conversion of fibrinogen to fibrin and also catalyzes the activation of protein C. Active protein C is able to proteolytically inactivate enhancers of the coagulation cascade.

c-Myc is a protein of the Myc family of transcription factors (c-Myc, B-Myc, L-Myc, N-Myc, and s-Myc) encoded by the MYC proto-oncogene. c-Myc was first discovered as the cellular homolog of the retroviral v-Myc oncogene. c-Myc is a transcription factor for genes involved in cell growth, proliferation, differentiation, and apoptosis. c-Myc contains a basic helix-loop-helix domain and a leucine zipper domain that allow for its heterodimerization with its binding partner Max. Myc/Max complexes are able to activate genes via the Myc transactivation domain (1).