Recombinant Human Nova1 protein is a Human Full Length protein, in the 2 to 507 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons (PubMed:10811881). Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord (By similarity).
RNA-binding protein Nova-1, Neuro-oncological ventral antigen 1, Onconeural ventral antigen 1, Paraneoplastic Ri antigen, Ventral neuron-specific protein 1, NOVA1
Recombinant Human Nova1 protein is a Human Full Length protein, in the 2 to 507 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 0.32% Tris HCl
The final product was refolded using a unique “temperature shift inclusion body refolding” technology and chromatographically purified.
Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons (PubMed:10811881). Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord (By similarity).
Nova1 also known as Neuro-oncological ventral antigen 1 is a member of the Nova family of RNA-binding proteins. It has a molecular mass of approximately 53 kDa. Nova1 is predominantly expressed in the nervous system with high presence in neurons. The protein plays a role in the regulation of alternative splicing by binding to specific RNA sequences. This binding activity influences the splicing of various pre-mRNA transcripts highlighting the role of Nova1 in post-transcriptional gene regulation.
Nova1 influences neuronal integrity by regulating RNA processing events. It binds to RNA motifs to ensure the accurate splicing needed for correct neuronal function. Nova1 functions as part of a multi-protein complex that includes spliceosomal components which help in recognizing splice sites in precursor RNA. The splicing activity of Nova1 affects the expression of numerous genes related to synaptic function and neurodevelopment which is critical for maintaining proper neuronal communication and plasticity.
Nova1 participates in the neuronal alternative splicing pathway and influences synaptic signaling pathways. Its activity affects the pathways by regulating the splicing of various genes critical for these pathways. For example Nova1 is involved with proteins like Nova2 within these pathways. Their combined roles ensure that various proteins essential for synaptic function are produced in the correct isoforms which is necessary for synaptic health and plasticity.
Nova1 has been linked to neurodevelopmental disorders and certain cancers such as brain tumors. It plays a role in these diseases by dysregulating the alternative splicing of transcripts necessary for normal neuronal development and tumor suppression. Nova1 interacts with other proteins such as hnRNP proteins in the context of these disorders which further modulates the disease process. Understanding Nova1's roles helps in developing therapeutic strategies that target aberrant splicing events in these conditions.
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