Acinus抗体

产品介绍background:
Chromatin condensation and nuclear fragmentation (CCNF) are the hallmarks of apoptosis. CCNF is triggered by the activation of members of the caspase family, caspase activated DNase (CAD/DFF40), and several novel proteins including AIF and CIDE. A new inducer of chromatin condensation was recently identified and designated Acinus (for apoptotic chromatin condensation inducer in the nucleus). Acinus is cleaved by Caspase 3 and an additional unknown protease generating a small active peptide p17, which causes chromatin condensation in vitro when it is added to purified nuclei. Acinus also induces apoptotic chromatin condensation in cells. Acinus is ubiquitously expressed. Three different spliced forms of Acinus have been identified in human and mouse and designated Acinus L (1341 amino acids), Acinus S (583 amino acids) and Acinus S' (614 amino acids)

Function:
Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells.

Subunit:
Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Forms heterodimers with RNPS1. Found in a heterotrimeric complex with ACIN1, RNPS1 and SAP18. Interacts with API5. Interacts with SRPK2 in a phosphorylation-dependent manner.

Subcellular Location:
Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.

Tissue Specificity:
Ubiquitous. The Ser-1180 phosphorylated form (by SRPK2) is highly expressed and phosphorylated in patients with myeloid hematologic malignancies.

Post-translational modifications:
Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1.
Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.

Similarity:
Contains 1 SAP domain.