Goat Anti-HTATSF1 Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | O43719 |
Other Accession | NP_055315, 27336, 317612 (rat) |
Reactivity | Human |
Predicted | Rat, Dog |
Host | Goat |
Clonality | Polyclonal |
Concentration | 100ug/200ul |
Isotype | IgG |
Calculated MW | 85853 Da |
Gene ID | 27336 |
---|---|
Other Names | HIV Tat-specific factor 1, Tat-SF1, HTATSF1 |
Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Goat Anti-HTATSF1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | HTATSF1 {ECO:0000303|PubMed:35597237, ECO:0000312|HGNC:HGNC:5276} |
---|---|
Function | Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch- site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint- interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S- phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). |
Cellular Location | Nucleus. Chromosome Note=Recruited to DNA damage sites during S-phase following interaction with poly-ADP-ribosylated RPA1. |
Tissue Location | Widely expressed.. |
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
The protein encoded by this gene functions as a cofactor for the stimulation of transcriptional elongation by HIV-1 Tat, which binds to the HIV-1 promoter through Tat-TAR interaction. This protein may also serve as a dual-function factor to couple transcription and splicing and to facilitate their reciprocal activation. Alternatively spliced transcript variants have been found for this gene.
References
DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation. Chen Y, et al. Genes Dev, 2009 Dec 1. PMID 19952111.
Tat-SF1 is not required for Tat transactivation but does regulate the relative levels of unspliced and spliced HIV-1 RNAs. Miller HB, et al. PLoS One, 2009 May 27. PMID 19479034.
Toward a confocal subcellular atlas of the human proteome. Barbe L, et al. Mol Cell Proteomics, 2008 Mar. PMID 18029348.
Large-scale mapping of human protein-protein interactions by mass spectrometry. Ewing RM, et al. Mol Syst Biol, 2007. PMID 17353931.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, et al. Cell, 2006 Nov 3. PMID 17081983.
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.