Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
SAP18 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O00422 |
|---|---|
| Clone Names | 100528183 |
| Gene ID | 10284 |
|---|---|
| Other Names | Histone deacetylase complex subunit SAP18, 18 kDa Sin3-associated polypeptide, 2HOR0202, Cell growth-inhibiting gene 38 protein, Sin3-associated polypeptide p18, SAP18 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SAP18 |
|---|---|
| Function | Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing- dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. |
| Cellular Location | Nucleus. Cytoplasm. Nucleus speckle. Note=Shuttles between the nucleus and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (PubMed:20966198). |
| Tissue Location | Ubiquitous. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
Histone acetylation plays a key role in the regulation ofeukaryotic gene expression. Histone acetylation and deacetylationare catalyzed by multisubunit complexes. The protein encoded bythis gene is a component of the histone deacetylase complex, whichincludes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and otherpolypeptides. This protein directly interacts with SIN3 andenhances SIN3-mediated transcriptional repression when tethered tothe promoter. A pseudogene has been identified on chromosome 2.
References
Sorin, M., et al. PLoS Pathog. 5 (6), E1000463 (2009) :McCallum, S.A., et al. Biochemistry 45(39):11974-11982(2006)Joselin, A.P., et al. J. Biol. Chem. 281(18):12475-12484(2006)Schwerk, C., et al. Mol. Cell. Biol. 23(8):2981-2990(2003)Koipally, J., et al. EMBO J. 18(11):3090-3100(1999)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
