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Mouse Anti-HNRNPA1 Recombinant Antibody (CBFYH-1622) (CBMAB-H0503-FY)

This product is mouse antibody that recognizes HNRNPA1. The antibody CBFYH-1622 can be used for immunoassay techniques such as: WB, ELISA, IF, IP, MA.
See all HNRNPA1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Cattle, Dog
Clone
CBFYH-1622
Antibody Isotype
IgG2a
Application
WB, ELISA, IF, IP, MA

Basic Information

Immunogen
Full length partially purified human hnRNP A1.
Specificity
Human, Mouse, Cattle, Dog
Antibody Isotype
IgG2a
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
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Heterogeneous Nuclear Ribonucleoprotein A1
Introduction
This gene encodes a member of a family of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs), which are RNA-binding proteins that associate with pre-mRNAs in the nucleus and influence pre-mRNA processing, as well as other aspects of mRNA metabolism and transport. The protein encoded by this gene is one of the most abundant core proteins of hnRNP complexes and plays a key role in the regulation of alternative splicing. Mutations in this gene have been observed in individuals with amyotrophic lateral sclerosis 20. Multiple alternatively spliced transcript variants have been found. There are numerous pseudogenes of this gene distributed throughout the genome.
Entrez Gene ID
Human3178
Mouse15382
Cattle505093
Dog102152026
UniProt ID
HumanP09651
MouseP49312
CattleP09867
DogE2QYP1
Alternative Names
Heterogeneous Nuclear Ribonucleoprotein A1; Single-Strand RNA-Binding Protein; Helix-Destabilizing Protein; HnRNP A1; HNRPA1; Putative Heterogeneous Nuclear Ribonucleoprotein A1-Like 3; Heterogeneous Nuclear Ribonucleoprotein Core Protein A1; Heterogeneous Nuclear Ribonucleoprotein A1B Protein; Heterogeneous Nuclear Ribonucleoprotein B2 Protein; Nuclear Ribonucleoprotein Particle A1 Protein
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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