Human HNRNPD ELISA Kit (V2LY-0626-LY4667)

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Basic Information

Sensitivity
0.0078 ng/mL
Detection Range
0.015-3 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
38.4 kDa
Components
  • Pre-coated ELISA plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

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

Storage
Store at 2-8°C
More Infomation

Target

Full Name
heterogeneous nuclear ribonucleoprotein D
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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