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Rabbit Anti-HNRNPD (Phosphorylated S83) Polyclonal Antibody (PTM-CBPAB-0766YC) (PTM-CBPAB-0766YC)

Provided herein is a Rabbit polyclonal antibody against Heterogeneous Nuclear Ribonucleoprotein D. The antibody can be used for immunoassay techniques, such as ICC, IF, IHC-P, WB.
See all HNRNPD antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Antibody Isotype
IgG
Application
ICC, IF, IHC-P, WB

Basic Information

Immunogen
Peptide sequence around phosphorylation site of Serine 83(N-S-S(p)-P-R) derived from Human hnRPD
Specificity
Human, Mouse
Antibody Isotype
IgG
Clonality
Monoclonal
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!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
heterogeneous nuclear ribonucleoprotein D
Introduction
HNRNPD belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants.
Entrez Gene ID
Human3184
Mouse11991
UniProt ID
HumanQ14103
MouseQ60668
Alternative Names
Heterogeneous Nuclear Ribonucleoprotein D; AU-Rich Element RNA Binding Protein 1, 37kDa; HnRNP D0; HNRPD; AUF1; Heterogeneous Nuclear Ribonucleoprotein D (AU-Rich Element RNA-Binding Protein 1, 37kD); Heterogeneous Nuclear Ribonucleoprotein D0;
Function
Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation.
Biological Process
3'-UTR-mediated mRNA destabilization Source: Ensembl
Cellular response to amino acid stimulus Source: Ensembl
Cellular response to estradiol stimulus Source: Ensembl
Cellular response to nitric oxide Source: Ensembl
Cellular response to putrescine Source: Ensembl
Cerebellum development Source: Ensembl
Circadian regulation of translation Source: UniProtKB
CRD-mediated mRNA stabilization Source: ComplexPortal
Hepatocyte dedifferentiation Source: Ensembl
Liver development Source: Ensembl
mRNA transcription by RNA polymerase II Source: BHF-UCL
Negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: ComplexPortal
Positive regulation of cytoplasmic translation Source: ComplexPortal
Positive regulation of telomerase RNA reverse transcriptase activity Source: BHF-UCL
Positive regulation of telomere capping Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of translation Source: UniProtKB
Regulation of circadian rhythm Source: UniProtKB
Regulation of gene expression Source: GO_Central
Regulation of telomere maintenance Source: BHF-UCL
Regulation of transcription, DNA-templated Source: UniProtKB
Response to calcium ion Source: Ensembl
Response to electrical stimulus Source: Ensembl
Response to rapamycin Source: Ensembl
Response to sodium phosphate Source: Ensembl
RNA catabolic process Source: ProtInc
RNA processing Source: ProtInc
Cellular Location
Nucleus; Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally.
PTM
Arg-345 is dimethylated, probably to asymmetric dimethylarginine.
Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-mediated methylation regulates tyrosine phosphorylation (By similarity).

Cui, X., Hao, C., Gong, L., Kajitani, N., & Schwartz, S. (2022). HnRNP D activates production of HPV16 E1 and E6 mRNAs by promoting intron retention. Nucleic Acids Research, 50(5), 2782-2806.

Hu, H., Zhang, H., Xing, Y., Zhou, Y., Chen, J., Li, C., ... & Huang, H. (2022). The lncRNA THOR interacts with and stabilizes hnRNPD to promote cell proliferation and metastasis in breast cancer. Oncogene, 41(49), 5298-5314.

Kumar, V., Kumar, A., Kumar, M., Lone, M. R., Mishra, D., & Chauhan, S. S. (2022). NFκB (RelA) mediates transactivation of hnRNPD in oral cancer cells. Scientific reports, 12(1), 5944.

Lin, J., Xie, Z., Zhang, Z., Li, M., Ye, G., Yu, W., ... & Shen, H. (2022). LncRNA MRF drives the regulatory function on monocyte recruitment and polarization through HNRNPD-MCP1 axis in mesenchymal stem cells. Journal of Biomedical Science, 29(1), 1-19.

Zhang, Q., Zhang, J., Ye, J., Li, X., Liu, H., Ma, X., ... & Liu, Q. (2021). Nuclear speckle specific hnRNP D-like prevents age-and AD-related cognitive decline by modulating RNA splicing. Molecular Neurodegeneration, 16, 1-19.

Yu, S., Ruan, X., Liu, X., Zhang, F., Wang, D., Liu, Y., ... & Xue, Y. (2021). HNRNPD interacts with ZHX2 regulating the vasculogenic mimicry formation of glioma cells via linc00707/miR-651-3p/SP2 axis. Cell Death & Disease, 12(2), 153.

Zhao, P., Ji, M. M., Fang, Y., Li, X., Yi, H. M., Yan, Z. X., ... & Zhao, W. L. (2021). A novel lncRNA TCLlnc1 promotes peripheral T cell lymphoma progression through acting as a modular scaffold of HNRNPD and YBX1 complexes. Cell Death & Disease, 12(4), 321.

Li, J., He, M., Xu, W., & Huang, S. (2019). LINC01354 interacting with hnRNP-D contributes to the proliferation and metastasis in colorectal cancer through activating Wnt/β-catenin signaling pathway. Journal of Experimental & Clinical Cancer Research, 38, 1-15.

Alfano, L., Caporaso, A., Altieri, A., Dell’Aquila, M., Landi, C., Bini, L., ... & Giordano, A. (2019). Depletion of the RNA binding protein HNRNPD impairs homologous recombination by inhibiting DNA-end resection and inducing R-loop accumulation. Nucleic Acids Research, 47(8), 4068-4085.

Latorre, E., Torregrossa, R., Wood, M. E., Whiteman, M., & Harries, L. W. (2018). Mitochondria-targeted hydrogen sulfide attenuates endothelial senescence by selective induction of splicing factors HNRNPD and SRSF2. Aging (Albany NY), 10(7), 1666.

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

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