Anti-Aurora A/Aurka Antibody Picoband®

AURKA (aurora kinase A), also called ARK1, AurA, AIK , AURORA2 , BTAK, PPP1R47, STK7, STK15, STK6, is a mitotic centrosomal protein kinase. The main role of AURKA in tumor development is in controlling chromosome segregation during mitosis. Aurora A is a member of a family of mitotic serine/threonine kinases. Cell cycle and Northern blot analyses showed that peak expression of AURKA occurs during the G2/M phase and then decreases. By fluorescence in situ hybridization, AURKA gene is represented by 2 signals in chromosome bands 20q13.2-q13.3 and 1q41-q42. The AURKA gene is overexpressed in many human cancers. Ectopic overexpression of Aurora kinase A in mammalian cells induces centrosome amplification, chromosome instability, and oncogenic transformation, a phenotype characteristic of loss-of-function mutations of p53. Depletion of Ajuba prevented activation of AURKA at centrosomes in late G2 phase and inhibited mitotic entry. Activation of AURKA was independently sufficient to induce rapid ciliary resorption, and AURKA acted in this process through phosphorylation of HDAC6, leading to HDAC6-dependent tubulin deacetylation and destabilization of the ciliary axoneme. Small molecule inhibitors of AURKA and HDAC6 reduced regulated disassembly of cilia.

Probable ATP-dependent RNA helicase DDX58;3.6.4.13; DEAD box protein 58; RIG-I-like receptor 1; RLR-1; Retinoic acid-inducible gene 1 protein; RIG-1; Retinoic acid-inducible gene I protein; RIG-I; DDX58

Antiviral Signaling, Chromatin Binding Proteins, DNA/RNA, DNA/RNA Binding, Epigenetics and Nuclear Signaling, Immune System Diseases, Immunology, RNA Processing

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'- triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length) . In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK- related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs) ; IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) . It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) . Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs) . May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. .

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.

Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cell junction, tight junction. Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.