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Mouse Anti-HNRNPU Recombinant Antibody (3C181) (CBMAB-R0548-CN)

This product is a Mouse antibody that recognizes HNRNPU. The antibody 3C181 can be used for immunoassay techniques such as: ICC, IF, IHC, IP, WB.
See all HNRNPU antibodies

Summary

Host Animal
Mouse
Specificity
Cattle, Human, Mouse, Pig, Rabbit, Rat
Clone
3C181
Antibody Isotype
IgG1, κ
Application
ICC, IF, IHC, IP, WB

Basic Information

Immunogen
M19 fusion protein containing full-length human protein
Specificity
Cattle, Human, Mouse, Pig, Rabbit, Rat
Antibody Isotype
IgG1, κ
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Preservative
0.09% Sodium azide

Target

Full Name
Heterogeneous Nuclear Ribonucleoprotein U
Introduction
This gene encodes a member of a family of proteins that bind nucleic acids and function in the formation of ribonucleoprotein complexes in the nucleus with heterogeneous nuclear RNA (hnRNA). The encoded protein has affinity for both RNA and DNA, and binds scaffold-attached region (SAR) DNA. Mutations in this gene have been associated with epileptic encephalopathy, early infantile, 54. A pseudogene of this gene has been identified on chromosome 14. [provided by RefSeq, Jun 2017]
Entrez Gene ID
Human3192
Mouse51810
Rat117280
Rabbit100348766
Cattle539950
Pig102165761
UniProt ID
HumanQ00839
MouseQ8VEK3
RatQ6IMY8
RabbitG1T7H0
CattleA2VDN7
PigF1S8L9
Alternative Names
Heterogeneous Nuclear Ribonucleoprotein U; Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A); Nuclear P120 Ribonucleoprotein; HNRNPU Antisense RNA 1; HnRNP U; GRIP120; HNRPU; SAF-A; U21.1; Pp120; SAFA;
Function
DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression (PubMed:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991, PubMed:25986610, PubMed:28622508).

Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability (PubMed:1324173, PubMed:8174554, PubMed:28622508).

Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity).

Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:8174554, PubMed:9353307, PubMed:10490622, PubMed:15711563, PubMed:19617346, PubMed:23811339).

Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner (PubMed:10490622, PubMed:15711563).

Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation (PubMed:10490622).

Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus (PubMed:19617346).

Negatively regulates glucocorticoid-mediated transcriptional activation (PubMed:9353307).

Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity).

Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (PubMed:23811339).

Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity).

Plays a role in the regulation of telomere length (PubMed:18082603).

Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991).

Plays a role in mRNA stability (PubMed:17174306, PubMed:17289661, PubMed:19029303).

Component of the CRD-mediated complex that promotes MYC mRNA stabilization (PubMed:19029303).

Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR) (PubMed:17174306).

Plays a role in mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610).

Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression (PubMed:21242313).

Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis (PubMed:25986610).

Contributes also to the targeting of AURKA to mitotic spindle MTs (PubMed:21242313).

Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365).

Binds to chromatin-associated RNAs (caRNAs) (PubMed:28622508).

Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:7509195, PubMed:1324173, PubMed:9204873, PubMed:9405365, PubMed:10671544, PubMed:11003645, PubMed:11909954, PubMed:28622508).

Binds to the Xist RNA (PubMed:26244333).

Binds the long non-coding H19 RNA (PubMed:23811339).

Binds to SMN1/2 pre-mRNAs at G/U-rich regions (PubMed:22325991).

Binds to small nuclear RNAs (snRNAs) (PubMed:22325991).

Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306).

Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (By similarity).

Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity).

Required for embryonic development (By similarity).

Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (By similarity).

(Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm.
Biological Process
Adaptive thermogenesis Source: UniProtKB
Cardiac muscle cell development Source: Ensembl
Cell cycle Source: UniProtKB-KW
Cell division Source: UniProtKB-KW
Cellular response to glucocorticoid stimulus Source: UniProtKB
Cellular response to leukemia inhibitory factor Source: UniProtKB
Circadian regulation of gene expression Source: UniProtKB
CRD-mediated mRNA stabilization Source: ComplexPortal
Dendritic transport of messenger ribonucleoprotein complex Source: Ensembl
Dosage compensation by inactivation of X chromosome Source: UniProtKB
Maintenance of protein location in nucleus Source: UniProtKB
mRNA splicing, via spliceosome Source: UniProtKB
mRNA stabilization Source: UniProtKB
Negative regulation of kinase activity Source: UniProtKB
Negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: ComplexPortal
Negative regulation of stem cell differentiation Source: UniProtKB
Negative regulation of telomere maintenance via telomerase Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Negative regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
Osteoblast differentiation Source: UniProtKB
Positive regulation of attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
Positive regulation of brown fat cell differentiation Source: UniProtKB
Positive regulation of cytoplasmic translation Source: ComplexPortal
Positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
Positive regulation of stem cell proliferation Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Protein localization to spindle microtubule Source: UniProtKB
Regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
Regulation of chromatin organization Source: UniProtKB
Regulation of mitotic cell cycle Source: UniProtKB
Regulation of mitotic spindle assembly Source: UniProtKB
RNA localization to chromatin Source: UniProtKB
RNA processing Source: ProtInc
Cellular Location
Centrosome; Spindle; Spindle pole; Nucleus; Nucleus matrix; Nucleus speckle; Cytoplasm; Chromosome; Kinetochore; Midbody; Cell surface; Cytoplasmic granule. Localizes at inactive X chromosome (Xi) regions (PubMed:11003645, PubMed:14608463, PubMed:15563465). Localizes in the nucleus during interphase (PubMed:21242313). At metaphase, localizes with mitotic spindle microtubules (MTs) (PubMed:21242313). At anaphase, localizes in the mitotic spindle midzone (PubMed:21242313). Localizes in spindle MTs proximal to spindle poles in a TPX2- and AURKA-dependent manner (PubMed:21242313). The Ser-59 phosphorylated form localizes to centrosomes during prophase and metaphase, to mitotic spindles in anaphase and to the midbody during cytokinesis (PubMed:25986610). Colocalizes with SMARCA4 in the nucleus (By similarity). Colocalizes with CBX5 in the nucleus (PubMed:19617346). Colocalizes with NR3C1 in nuclear speckles (PubMed:9353307). Localized in cytoplasmic ribonucleoprotein (RNP) granules containing untranslated mRNAs (PubMed:17289661).
Involvement in disease
Developmental and epileptic encephalopathy 54 (DEE54):
A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
PTM
Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities (PubMed:9405365, PubMed:10671544).
Extensively phosphorylated (PubMed:7993898). Phosphorylated on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis (PubMed:25986610).
Arg-739 is dimethylated, probably to asymmetric dimethylarginine (Ref. 8). Arg-733 is dimethylated, probably to asymmetric dimethylarginine (By similarity).
Citrullinated by PADI4.

Marenda, M., Lazarova, E., & Gilbert, N. (2022). The role of SAF-A/hnRNP U in regulating chromatin structure. Current Opinion in Genetics & Development, 72, 38-44.

Shi, Z. D., Hao, L., Han, X. X., Wu, Z. X., Pang, K., Dong, Y., ... & Han, C. H. (2022). Targeting HNRNPU to overcome cisplatin resistance in bladder cancer. Molecular cancer, 21(1), 37.

Sapir, T., Kshirsagar, A., Gorelik, A., Olender, T., Porat, Z., Scheffer, I. E., ... & Reiner, O. (2022). Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the developing mouse cortex. Nature communications, 13(1), 4209.

Pan, J., Tang, Y., Liu, S., Li, L., Yu, B., Lu, Y., & Wang, Y. (2020). LIMD1‐AS1 suppressed non‐small cell lung cancer progression through stabilizing LIMD1 mRNA via hnRNP U. Cancer Medicine, 9(11), 3829-3839.

Durkin, A., Albaba, S., Fry, A. E., Morton, J. E., Douglas, A., Beleza, A., ... & Balasubramanian, M. (2020). Clinical findings of 21 previously unreported probands with HNRNPU‐related syndrome and comprehensive literature review. American Journal of Medical Genetics Part A, 182(7), 1637-1654.

Zietzer, A., Hosen, M. R., Wang, H., Goody, P. R., Sylvester, M., Latz, E., ... & Jansen, F. (2020). The RNA-binding protein hnRNPU regulates the sorting of microRNA-30c-5p into large extracellular vesicles. Journal of extracellular vesicles, 9(1), 1786967.

Xing, S., Li, Z., Ma, W., He, X., Shen, S., Wei, H., ... & Zhang, H. (2019). DIS3L2 promotes progression of hepatocellular carcinoma via hnRNP U-mediated alternative splicing. Cancer research, 79(19), 4923-4936.

Zhang, L., Song, D., Zhu, B., & Wang, X. (2019, June). The role of nuclear matrix protein HNRNPU in maintaining the architecture of 3D genome. In Seminars in Cell & Developmental Biology (Vol. 90, pp. 161-167). Academic Press.

Izumi, H., & Funa, K. (2019). Telomere function and the G-quadruplex formation are regulated by hnRNP U. Cells, 8(5), 390.

Fan, H., Lv, P., Huo, X., Wu, J., Wang, Q., Cheng, L., ... & Wen, B. (2018). The nuclear matrix protein HNRNPU maintains 3D genome architecture globally in mouse hepatocytes. Genome Research, 28(2), 192-202.

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

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