CPSF6 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, E |
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Primary Accession | Q16630 |
Other Accession | Q6DDW4, Q6NVF9, Q6NWC6, Q5ZL34, Q0P5D2, NP_008938.2 |
Reactivity | Human |
Predicted | Bovine, Chicken, Zebrafish, Mouse, Xenopus |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 59210 Da |
Antigen Region | 23-51 aa |
Gene ID | 11052 |
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Other Names | Cleavage and polyadenylation specificity factor subunit 6, Cleavage and polyadenylation specificity factor 68 kDa subunit, CFIm68, CPSF 68 kDa subunit, Pre-mRNA cleavage factor Im 68 kDa subunit, Protein HPBRII-4/7, CPSF6, CFIM68 |
Target/Specificity | This CPSF6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 23-51 amino acids from the N-terminal region of human CPSF6. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | CPSF6 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CPSF6 (HGNC:13871) |
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Function | Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'- UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:21295486, PubMed:29276085). Plays a role in mRNA export (PubMed:19864460). |
Cellular Location | Nucleus. Nucleus, nucleoplasm. Nucleus speckle. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). Colocalizes with PSPC1 in punctate subnuclear structures often located adjacent to nuclear speckles, called paraspeckles, and corresponding to interchromatin granules-associated zones (IGAZs) (PubMed:17267687). Distribution in speckles and paraspeckles varies during the cell cycle (PubMed:17267687). Associates at sites of active transcription on nascent perichromatin fibrils (PFs) and perichromatin granules (PubMed:17267687). Nuclear import is mediated via interaction with TNPO3 independently of CPSF6 phosphorylation status (PubMed:30916345). |

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Background
The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. The cleavage factor complex is composed of four polypeptides. This gene encodes the 68kD subunit. It has a domain organization reminiscent of spliceosomal proteins.
References
Lee, K., et al. Cell Host Microbe 7(3):221-233(2010)
Ruepp, M.D., et al. Mol. Biol. Cell 20(24):5211-5223(2009)
Xin, X., et al. Genome Res. 19(7):1262-1269(2009)
Maggi, L.B. Jr., et al. Mol. Cell. Biol. 28(23):7050-7065(2008)
Gudbjartsson, D.F., et al. Nat. Genet. 40(5):609-615(2008)

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