HNRNPA1 Antibodies

Background

HNRNPA1 is a nuclear RNA-binding protein widely expressed in mammalian cells, and it is an important member of the heterogeneous nuclear ribonucleoprotein family. This protein mainly participates in the processing, maturation, and transport of precursor mRNAs. It regulates alternative splicing, mRNA stability, and nuclear-cytoplasmic export by recognizing specific RNA sequences. Under cellular stress conditions, HNRNPA1 can undergo cytoplasmic redistribution and participate in the formation of stress granules, helping cells adapt to environmental changes. This protein was first identified and purified in the 1980s. Its structural characteristics, including two highly conserved RNA recognition motifs (RRM) and a glycine-rich RGG domain, provide an ideal model for studying RNA-protein interactions. Subsequent studies have revealed that it plays a key role in the pathological mechanisms of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Mutations or abnormal aggregation of HNRNPA1 can directly participate in the occurrence of the disease. In-depth exploration of HNRNPA1 not only expands our understanding of the RNA metabolic regulatory network but also provides important theoretical basis for targeted treatment of related diseases.

Structure Function Application Advantage Our Products

Structure of HNRNPA1

HNRNPA1 is a RNA-binding protein with a molecular weight of approximately 34 kDa. It is highly conserved across different species and is involved in fundamental biological processes such as RNA processing, splicing, and transport.

Species	Human	Mouse	Rat	Pig	Cow
Molecular Weight (kDa)	34	34	34	34	34
Primary Structural Differences	Sequence highly conserved	Homology with humans > 98%	Homology with humans > 98%	Homology with humans > 97%	Homology with humans > 97%

HNRNPA1 is highly conserved among different species, with a nearly identical molecular weight. The functional differences of HNRNPA1 mainly result from the regulation of expression levels and post-translational modifications, rather than significant changes in the amino acid sequence.

Fig. 1 Schematic diagram showing the protein domain organization of HNRNPA1.¹

Key structural properties of HNRNPA1:

Two RNA recognition motifs (RRM1 and RRM2), responsible for binding RNA
C-terminal glycine-rich domain (RGG box), mediating protein interactions
Nuclear localization signal sequence, regulating nuclear-cytoplasmic shuttling
Multiple post-translational modification sites, regulating its function

Functions of HNRNPA1

HNRNPA1 is a versatile RNA-binding protein that is mainly involved in all aspects of RNA metabolism and plays a central role in gene expression regulation.

Function	Description
RNA Splicing Regulation	Participates in the selective splicing of pre-mRNA, determining the retention or skipping of specific exons, and influencing protein diversity.
mRNA Transport	Mediates the transport of mature mRNA from the nucleus to the cytoplasm, ensuring smooth translation.
Transcription Regulation	Influences the transcriptional activity of specific genes through interaction with DNA or transcription factors.
Stress Granule Formation	Participates in stress granule assembly, protects mRNA and regulates its translation under cellular stress conditions.
Telomere Maintenance	Associates with telomere RNA, participating in the regulation of telomere length and chromosome end protection.

Applications of HNRNPA1 and HNRNPA1 Antibody in Literature

1. Lian, Cheng, et al. "Epigenetic reader ZMYND11 noncanonical function restricts HNRNPA1-mediated stress granule formation and oncogenic activity." Signal transduction and targeted therapy 9.1 (2024): 258. https://doi.org/10.1038/s41392-024-01961-7

The article indicates that ZMYND11 inhibits the formation of stress granules and the ratio of PKM2/PKM1 by recognizing methylated HNRNPA1 and promoting its nuclear retention, thereby exerting its tumor-suppressing effect. Tumors with low expression of ZMYND11 are sensitive to PRMT5 inhibitors, providing a new therapeutic target.

2. Li, Wen-juan, et al. "Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth." Nature communications 12.1 (2021): 1946. https://doi.org/10.1038/s41467-021-21963-1

The article indicates that PRMT4/5/7 mediate arginine methylation of hnRNPA1, regulating its RNA binding and alternative splicing. All three are upregulated in cancer cells, and their combined inhibition has a synergistic effect, providing new targets for cancer treatment.

3. Liu, DongWei, et al. "HNRNPA1-mediated exosomal sorting of miR-483-5p out of renal tubular epithelial cells promotes the progression of diabetic nephropathy-induced renal interstitial fibrosis." Cell death & disease 12.3 (2021): 255. https://doi.org/10.1038/s41419-021-03460-x

The article indicates that HNRNPA1 mediates the extracellular vesicle sorting of miR-483-5p, allowing it to be transported from renal tubular epithelial cells into urine, thereby relieving the inhibition on MAPK1 and TIMP2, and thereby promoting renal interstitial fibrosis in diabetic nephropathy.

4. Wang, Tianqi, et al. "Lactate-driven lactylation of HNRNPA1 orchestrates PKM2 splicing and glycolytic reprogramming in bladder cancer." Journal of Experimental & Clinical Cancer Research (2025). https://doi.org/10.1186/s13046-025-03591-5

The article indicates that lactic acid drives the lysyl modification of lysine at position 350 of HNRNPA1 mediated by P300, which promotes the splicing of the PKM gene into the PKM2 subtype, enhances glycolysis, and promotes the progression of bladder cancer. Targeting this process holds therapeutic potential.

5. Li, Chuling, et al. "RNA‐Binding Protein Hnrnpa1 Triggers Daughter Cardiomyocyte Formation by Promoting Cardiomyocyte Dedifferentiation and Cell Cycle Activity in a Post‐Transcriptional Manner." Advanced Science 12.2 (2025): 2402371. https://doi.org/10.1002/advs.202402371

The article indicates that HNRNPA1 regulates the splicing of METTL3, inhibits the m6A-dependent degradation of Pbx1/E2F1, promotes cardiomyocyte dedifferentiation and division, forms daughter cells, and improves post-myocardial infarction repair.

Creative Biolabs: HNRNPA1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality HNRNPA1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom HNRNPA1 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our HNRNPA1 antibodies, custom preparations, or technical support, contact us at email.

Reference

Lian, Cheng, et al. "Epigenetic reader ZMYND11 noncanonical function restricts HNRNPA1-mediated stress granule formation and oncogenic activity." Signal transduction and targeted therapy 9.1 (2024): 258. Distributed under Open Access license CC BY 4.0, and cropped from the original figure. https://doi.org/10.1038/s41392-024-01961-7