Rabbit Anti-HNRNPL Recombinant Antibody (EG1535) (CBMAB-EN1834-LY)

Name: Rabbit Anti-HNRNPL Recombinant Antibody (EG1535)
SKU: CBMAB-EN1834-LY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

EG1535

Application

WB: 1:500~1:1000 IHC: 1:50~1:100 IF: 1:100~1:500 ELISA: 1:20000

Immunogen

The antibody was produced against synthesized peptide derived from N-terminal of human hnRNP L.

Specificity

Human, Mouse

Antibody Isotype

IgG

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

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

heterogeneous nuclear ribonucleoprotein L

Introduction

Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene.

Entrez Gene ID

Human	3191
Mouse	15388

UniProt ID

Human	P14866
Mouse	Q8R081

Alternative Names

HNRPL; hnRNP-L; P/OKcl.14

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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Isotype control

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

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