Human HNRNPL ELISA Kit (V2LY-0626-LY3600)

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Basic Information

Sensitivity
0.23 ng/mL
Detection Range
0.5-150 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
64.1 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 L
Function
Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023).

Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284).

Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897).

As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841).
Biological Process
mRNA processing Source: InterPro
Negative regulation of transcription, DNA-templated Source: UniProtKB
Regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
Regulation of RNA splicing Source: GO_Central
RNA processing Source: ProtInc
Cellular Location
Nucleoplasm; Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules.
PTM
Several isoelectric forms of the L protein are probably the results of post-translational modifications.
Phosphorylation at Ser-544 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization.

Zhou, X., Zou, L., Liao, H., Luo, J., Yang, T., Wu, J., ... & Mao, X. (2022). Abrogation of HnRNP L enhances anti-PD-1 therapy efficacy via diminishing PD-L1 and promoting CD8+ T cell-mediated ferroptosis in castration-resistant prostate cancer. Acta Pharmaceutica Sinica B, 12(2), 692-707.

Bhattacharya, S., Wang, S., Reddy, D., Shen, S., Zhang, Y., Zhang, N., ... & Li, F. (2021). Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing. Nature Communications, 12(1), 6452.

Alexander, M. S., Hightower, R. M., Reid, A. L., Bennett, A. H., Iyer, L., Slonim, D. K., ... & Draper, I. (2021). hnRNP L is essential for myogenic differentiation and modulates myotonic dystrophy pathologies. Muscle & nerve, 63(6), 928-940.

Lu, J., Zhong, C., Luo, J., Shu, F., Lv, D., Liu, Z., ... & Mao, X. (2021). HnRNP-L-regulated circCSPP1/miR-520h/EGR1 axis modulates autophagy and promotes progression in prostate cancer. Molecular Therapy-Nucleic Acids, 26, 927-944.

Li, Y., Chen, B., Zhao, J., Li, Q., Chen, S., Guo, T., ... & Huang, S. (2021). HNRNPL circularizes ARHGAP35 to produce an oncogenic protein. Advanced Science, 8(13), 2001701.

Gu, J., Chen, Z., Chen, X., & Wang, Z. (2020). Heterogeneous nuclear ribonucleoprotein (hnRNPL) in cancer. Clinica Chimica Acta, 507, 286-294.

Zhao, Y., Zhou, J., He, L., Li, Y., Yuan, J., Sun, K., ... & Wang, H. (2019). MyoD induced enhancer RNA interacts with hnRNPL to activate target gene transcription during myogenic differentiation. Nature communications, 10(1), 5787.

Kishor, A., Ge, Z., & Hogg, J. R. (2019). hnRNP L‐dependent protection of normal mRNAs from NMD subverts quality control in B cell lymphoma. The EMBO Journal, 38(3), e99128.

Song, X., Xu, P., Meng, C., Song, C., Blackwell, T. S., Li, R., ... & Lv, C. (2019). lncITPF promotes pulmonary fibrosis by targeting hnRNP-L depending on its host gene ITGBL1. Molecular Therapy, 27(2), 380-393.

McClory, S. P., Lynch, K. W., & Ling, J. P. (2018). HnRNP L represses cryptic exons. Rna, 24(6), 761-768.

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

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