Antibody database

Heat shock cognate 71 kDa protein (Hsc70), also known as HSPA8, is a member of the heat shock protein 70 family (Hsp70). Unlike Hsp70, it is a constitutively expressed chaperone protein and is involved in diverse cellular processes including protein folding and protein degradation. Hsc70 consists of two domains: the nucleotide binding domain (NBD) and the substrate binding domain (SBD). Hsc70, with the help of accessory proteins, exerts its chaperone activity by binding to short hydrophobic stretches of nascent or unfolded polypeptides through the SBD in an ATP-dependent manner.

Human leukocyte antigen G (HLA G) is a major histocompatibility complex (MHC) class I molecule that is primarily expressed in the placenta and is essential for the immune tolerance of the fetus during pregnancy. Unlike many HLA genes, HLA G has relatively few variants and is alternatively spliced into seven different isoforms. Of these isoforms four are membrane-bound while three are predicted to be soluble. Both the membrane-bound and soluble form of HLA G can induce immune tolerance by binding to inhibitory receptors on various immune cells including macrophages and monocytes.

Atg12 is a ubiquitin-like protein that plays an essential role in cellular homeostasis by regulating the degradation and recycling of cytoplasmic organelles and macromolecules. Atg12 is one of two ubiquitin-like protein systems that is required during the early steps of autophagosome formation. Upon the initiation of phagopore assembly Atg12 is activated by binding to the E1-like enzyme Atg7 and is then transferred to the E2 enzyme Atg10.

Cluster of differentiation 74 (CD74) is an important integral membrane protein that serves as a chaperone for MHC class II molecules. CD74, also known as the invariant chain or Ii, is needed for the proper folding and trafficking of MHC class II in antigen presenting cells. CD74 serves as a scaffold for MHC class II assembly. During assembly CD74 blocks the peptide binding cleft of MHC class II to prevent binding of antigenic peptides.

Mucin 1 (Muc1) is a heavily glycosylated protein that coats mucosal epithelial cells of the lungs, intestines, and other organs. Muc1 is thought to protect cells by binding to pathogens and responding to infections. During trafficking to the plasma membrane Muc1 is proteolytically cleaved in the endoplasmic reticulum to form a stable heterodimeric complex of two fragments. The smaller C-terminal region contains the cytoplasmic tail and transmembrane domain and is non-covalently bound to the larger glycosylated extracellular domain.

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.