CPSF5 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O43809 |
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Clone Names | 5082554 |
Gene ID | 11051 |
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Other Names | Cleavage and polyadenylation specificity factor subunit 5, Cleavage and polyadenylation specificity factor 25 kDa subunit, CFIm25, CPSF 25 kDa subunit, Nucleoside diphosphate-linked moiety X motif 21, Nudix motif 21, Pre-mRNA cleavage factor Im 25 kDa subunit, NUDT21, CFIM25, CPSF25, CPSF5 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1915a was selected from the Center region of human CPSF5. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
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 | NUDT21 (HGNC:13870) |
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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:9659921, PubMed:8626397, PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085). 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:9659921, PubMed:8626397, PubMed:14690600, PubMed:17024186). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:17098938, 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:17098938, PubMed:20695905, PubMed:29276085). NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085). Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'- end processing (PubMed:8626397, PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:22813749, PubMed:20479262). The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (PubMed:20479262, PubMed:21295486). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629). |
Cellular Location | Nucleus. 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) In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles (PubMed:15169763) |
Tissue Location | Expressed in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas |
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Provided below are standard protocols that you may find useful for product applications.
Background
CPSF5 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 recruitement of other processing factors. CPSF5 is the 25kD subunit of the protein complex, which is composed of four polypeptides.
References
Dettwiler, S., et al., J. Biol. Chem. 279(34):35788-35797 (2004).Lehner, B., et al., Genome Res. 14(7):1315-1323 (2004).de Vries, H., et al., EMBO J. 19(21):5895-5904 (2000).Ruegsegger, U., et al., Mol. Cell 1(2):243-253 (1998).Ruegsegger, U., et al., J. Biol. Chem. 271(11):6107-6113 (1996).
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