Mouse Anti-CPSF6 Recombinant Antibody (CBFYC-2168) (V2LY-1206-LY995)

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Basic Information

Host Animal
Mouse
Clone
CBFYC-2168
Application
ELISA, IF, WB
Immunogen
CPSF6 (aa37-136) partial recombinant protein.
Host Species
Mouse
Specificity
Human, Mouse
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
IF(ICC)10 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
Batch dependent
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
More Infomation

Target

Full Name
cleavage and polyadenylation specific factor 6, 68kDa
Entrez Gene ID
Human11052
Mouse432508
UniProt ID
HumanQ16630
MouseQ6NVF9
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: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).

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:29276085, PubMed:21295486).

Plays a role in mRNA export (PubMed:19864460).

(Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and might thereby promote the integration of the virus in the nucleus of dividing cells (in vitro).
Biological Process
Messenger ribonucleoprotein complex assembly Source: UniProtKB
mRNA alternative polyadenylation Source: UniProtKB
mRNA processing Source: UniProtKB
Positive regulation of RNA export from nucleus Source: UniProtKB
Pre-mRNA cleavage required for polyadenylation Source: UniProtKB
Protein heterotetramerization Source: UniProtKB
Protein tetramerization Source: UniProtKB
Cellular Location
Nucleus; Nucleoplasm; Nucleus speckle; Cytoplasm. 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).
PTM
Phosphorylated (PubMed:29276085). Phosphorylated in the Arg/Ser-rich domain by SRPK1, in vitro (PubMed:29276085).
Symmetrically dimethylated on arginine residues in the GAR motif by PRMT5 in a WDR77- and CLNS1A-dependent manner (PubMed:20562214). Asymmetrically dimethylated on arginine residues in the GAR motif by PRMT1 (PubMed:20562214).

Zheng, Y., Schubert, H. L., Singh, P. K., Martins, L. J., Engelman, A. N., D’Orso, I., ... & Planelles, V. (2021). Cleavage and Polyadenylation Specificity Factor 6 Is Required for Efficient HIV-1 Latency Reversal. Mbio, 12(3), e01098-21.

Tan, S., Zhang, M., Shi, X., Ding, K., Zhao, Q., Guo, Q., ... & Zhao, X. (2021). CPSF6 links alternative polyadenylation to metabolism adaption in hepatocellular carcinoma progression. Journal of Experimental & Clinical Cancer Research, 40(1), 1-16.

Han, X., Jin, C., Zheng, G., Li, Y., Wang, Y., Zhang, E., ... & Cai, Z. (2021). Acute myeloid leukemia with CPSF6–RARG fusion resembling acute promyelocytic leukemia with extramedullary infiltration. Therapeutic advances in hematology, 12, 2040620720976984.

Zhong, Z., Ning, J., Boggs, E. A., Jang, S., Wallace, C., Telmer, C., ... & Ambrose, Z. (2021). Cytoplasmic CPSF6 regulates HIV-1 capsid trafficking and infection in a cyclophilin A-dependent manner. MBio, 12(2), e03142-20.

Wang, X., Xu, P., Cheng, F., Li, Y., Wang, Z., Hao, S., ... & Qiu, J. (2020). Cellular cleavage and polyadenylation specificity factor 6 (CPSF6) mediates nuclear import of human bocavirus 1 NP1 protein and modulates viral capsid protein expression. Journal of Virology, 94(2), e01444-19.

Achuthan, V., Perreira, J. M., Ahn, J. J., Brass, A. L., & Engelman, A. N. (2019). Capsid-CPSF6 interaction: Master regulator of nuclear HIV-1 positioning and integration. Journal of life sciences (Westlake Village, Calif.), 1(1), 39.

Jang, S., Cook, N. J., Pye, V. E., Bedwell, G. J., Dudek, A. M., Singh, P. K., ... & Engelman, A. N. (2019). Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. Nucleic acids research, 47(9), 4663-4683.

Bejarano, D. A., Peng, K., Laketa, V., Börner, K., Jost, K. L., Lucic, B., ... & Kräusslich, H. G. (2019). HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex. Elife, 8, e41800.

Qin, Y. Z., Huang, X. J., & Zhu, H. H. (2018). Identification of a novel CPSF6-RARG fusion transcript in acute myeloid leukemia resembling acute promyelocytic leukemia. Leukemia, 32(10), 2285-2287.

Sasado, T., Kondoh, H., Furutani-Seiki, M., & Naruse, K. (2017). Mutation in cpsf6/CFIm68 (cleavage and polyadenylation specificity factor subunit 6) causes short 3'UTRs and disturbs gene expression in developing embryos, as revealed by an analysis of primordial germ cell migration using the medaka mutant naruto. PloS one, 12(3), e0172467.

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For research use only. Not intended for any clinical use.

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