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Mouse Anti-HNRNPA1 Recombinant Antibody (2E6) (CBMAB-A3997-LY)

The product is antibody recognizes HNRPA1. The antibody 2E6 immunoassay techniques such as: WB, ELISA.
See all HNRNPA1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
2E6
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
HNRPA1 (AAH33714.1, 1 a.a. ~ 320 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
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!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Heterogeneous Nuclear Ribonucleoprotein A1
Introduction
This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA 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 is one of the most abundant core proteins of hnRNP complexes and it is localized to the nucleoplasm. This protein, along with other hnRNP proteins, is exported from the nucleus, probably bound to mRNA, and is immediately re-imported. Its M9 domain acts as both a nuclear localization and nuclear export signal. The encoded protein is involved in the packaging of pre-mRNA into hnRNP particles, transport of poly A+ mRNA from the nucleus to the cytoplasm, and may modulate splice site selection. It is also thought have a primary role in the formation of specific myometrial protein species in parturition. Multiple alternatively spliced transcript variants have been found for this gene but only two transcripts are fully described. These variants have multiple alternative transcription initiation sites and multiple polyA sites. [provided by RefSeq]
Entrez Gene ID
3178
UniProt ID
P09651
Alternative Names
HNRPA1; MGC102835
Function
Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836).

Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808).

Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791).

May bind to specific miRNA hairpins (PubMed:28431233).

(Microbial infection) May play a role in HCV RNA replication.

(Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis.
Biological Process
Cellular response to glucose starvation Source: CAFA
Cellular response to sodium arsenite Source: UniProtKB
Import into nucleus Source: HGNC-UCL
mRNA splicing, via spliceosome Source: UniProtKB
mRNA transport Source: UniProtKB-KW
Negative regulation of telomere maintenance via telomerase Source: BHF-UCL
Nuclear export Source: HGNC-UCL
Positive regulation of telomere maintenance via telomerase Source: BHF-UCL
Regulation of alternative mRNA splicing, via spliceosome Source: CAFA
RNA export from nucleus Source: HGNC-UCL
Cellular Location
Nucleus; Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:17289661).
Cytoplasm. (Microbial infection) In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner.
Nucleus. (Microbial infection) SARS coronavirus-2/SARS-CoV-2 ORF6 protein increases accumulation to the nucleus.
Involvement in disease
Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3):
An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
Amyotrophic lateral sclerosis 20 (ALS20):
A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
PTM
Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.
Sumoylated.

Zhang, D., Tao, L., Xu, N., Lu, X., Wang, J., He, G., ... & Chu, J. (2022). CircRNA circTIAM1 promotes papillary thyroid cancer progression through the miR-646/HNRNPA1 signaling pathway. Cell Death Discovery, 8(1), 21.

Han, X., Zhan, F., Yao, Y., Cao, L., Liu, J., & Yao, S. (2022). Clinical heterogeneity in a family with flail arm syndrome and review of hnRNPA1‐related spectrum. Annals of Clinical and Translational Neurology, 9(12), 1910-1917.

Li, W. J., He, Y. H., Yang, J. J., Hu, G. S., Lin, Y. A., Ran, T., ... & Liu, W. (2021). Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth. Nature communications, 12(1), 1946.

Martin, E. W., Thomasen, F. E., Milkovic, N. M., Cuneo, M. J., Grace, C. R., Nourse, A., ... & Mittag, T. (2021). Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation. Nucleic acids research, 49(5), 2931-2945.

Fu, R., Yang, P., Amin, S., & Li, Z. (2020). A novel miR-206/hnRNPA1/PKM2 axis reshapes the Warburg effect to suppress colon cancer growth. Biochemical and Biophysical Research Communications, 531(4), 465-471.

Sun, Y., Zhao, K., Xia, W., Feng, G., Gu, J., Ma, Y., ... & Li, D. (2020). The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure. Nature communications, 11(1), 6349.

Lan, Z., Yao, X., Sun, K., Li, A., Liu, S., & Wang, X. (2020). The interaction between lncRNA SNHG6 and hnRNPA1 contributes to the growth of colorectal cancer by enhancing aerobic glycolysis through the regulation of alternative splicing of PKM. Frontiers in oncology, 10, 363.

Gui, X., Luo, F., Li, Y., Zhou, H., Qin, Z., Liu, Z., ... & Li, D. (2019). Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly. Nature communications, 10(1), 2006.

Chen, Y., Liu, J., Wang, W., Xiang, L., Wang, J., Liu, S., ... & Guo, Z. (2018). High expression of hnRNPA1 promotes cell invasion by inducing EMT in gastric cancer. Oncology reports, 39(4), 1693-1701.

Kattimani, Y., & Veerappa, A. M. (2018). Complex interaction between mutant HNRNPA1 and gE of varicella zoster virus in pathogenesis of multiple sclerosis. Autoimmunity, 51(4), 147-151.

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

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