Mouse Polyclonal ZCH11 antibody. Carrier free. Suitable for WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human TUT4.
pH: 7.4
Constituents: 100% PBS
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Human | Tested |
Species | Dilution info | Notes |
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Species Human | Dilution info 1 µg/mL | Notes - |
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Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:25480299, PubMed:31036859). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (By similarity). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also functions as an integral regulator of microRNA biogenesis using 3 different uridylation mechanisms (PubMed:25979828). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (PubMed:19703396). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:25979828). Adds oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (PubMed:25979828). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP (PubMed:16643855). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (By similarity) (PubMed:16643855, PubMed:18172165, PubMed:19703396, PubMed:25480299, PubMed:25979828). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (PubMed:30122351).
KIAA0191, ZCCHC11, TUT4, Terminal uridylyltransferase 4, TUTase 4, Zinc finger CCHC domain-containing protein 11
Mouse Polyclonal ZCH11 antibody. Carrier free. Suitable for WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human TUT4.
pH: 7.4
Constituents: 100% PBS
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ZCH11 also known as Zinc Finger C2H2 11 is a protein that mechanically functions as a transcription factor. It has a molecular mass of approximately 72 kDa. ZCH11 is expressed in various tissues with higher levels observed in the liver and brain. This protein contains zinc finger motifs which help it bind to specific DNA sequences allowing it to influence the transcription of target genes.
ZCH11 plays an important role in regulating gene expression impacting cellular differentiation and development. It acts as an important element in cellular processes and is often part of larger protein complexes that collaborate to control transcription. Through its function as a transcription factor ZCH11 contributes to the maintenance of cellular homeostasis and is essential for normal cellular function.
ZCH11 is actively involved in the Wnt signaling and cell cycle regulation pathways. In the Wnt signaling pathway ZCH11 interacts with proteins such as β-catenin influencing gene expression related to cell proliferation and differentiation. In the context of cell cycle regulation ZCH11 interacts with cyclins and cyclin-dependent kinases ensuring proper progression through various phases of the cell cycle.
ZCH11 has connections to colorectal cancer and neurodegenerative diseases. Abnormal expression of ZCH11 may lead to the dysregulation of the Wnt signaling pathway contributing to the development of colorectal cancer. In neurodegenerative diseases ZCH11 may alter neuronal gene expression potentially leading to disease progression. In these cases ZCH11 shows relationships with proteins like APC (adenomatous polyposis coli) in cancer and tau protein in neurodegenerative conditions.
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All lanes: Western blot - Anti-ZCH11 antibody (ab89165) at 1 µg/mL
All lanes: Human spleen tissue lysate at 50 µg
Predicted band size: 185 kDa
Observed band size: 185 kDa
All lanes: Western blot - Anti-ZCH11 antibody (ab89165) at 1 µg/mL
Lane 1: ZCH11 transfected 293T cell lysate at 25 µg
Lane 2: Non transfected 293T cell lysate at 25 µg
Predicted band size: 185 kDa
Image collected and cropped by CiteAb under a CC-BY license from the publication
ZCH11 western blot using anti-ZCH11 antibody ab89165. Publication image and figure legend from Plé, H., Landry, P., et al., 2012, PLoS One, PubMed 23226537.
ab89165 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab89165 please see the product overview.
Platelets possess microRNA terminal nucleotidyltransferase activity.(A–B) Uridylation (A) and adenylation (B) assays were performed by incubating synthetic miR-223 or let-7a mature microRNAs or microRNA duplexes with protein extracts, prepared from Meg-01 cells or platelets isolated from 3 healthy volunteers, in the presence of α-32P-labeled UTP or ATP respectively, at 30°C for 90 min. Uridylated or adenylated forms of microRNAs were detected by denaturing PAGE and autoradiography. (C) Western blot detection of TUT4 uridyltransferase (left panel) and GLD2 adenyltransferase (right panel) enzymes in Meg-01 and platelet extracts using anti-TUT4 and anti-GLD2 antibodies, respectively.
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