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Validated All-in-One™ qPCR Primer for TARDBP(NM_007375.4) Search again
Product ID:
HQP171546
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ALS10, TDP-43
Gene Description:
TAR DNA binding protein
Target Gene Accession:
NM_007375.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle.
Gene References into function
- The dissection of the RNA binding properties of TDP-43 and their functional implications in relationship with the splicing process is reported
- Through the analysis of TDP, a protein functional in both transcriptional repression and alternative splicing, we have identified a new category of nuclear bodies within which the TDP molecules reside.
- the C-terminal region of TDP-43 is capable of binding directly to several proteins of the heterogeneous nuclear ribonucleoprotein (hnRNP) family with well known splicing inhibitory activity, in particular, hnRNP A2/B1 and hnRNP A1
- findings showed that TDP-43 is the major disease protein in frontotemporal lobar degeneration and amyotrophic lateral sclerosis; it was recovered only from affected central nervous system regions
- familial aggregation & clinical presentation of frontotemporal dementia + motor neuron disease; TDP-43 antibody stained neuronal inclusions similar in distribution & morphology to neuronal cytoplasmatic inclusions & neuronal intranuclear inclusions
- TDP-43 proteinopathy is the common pathologic substrate linking frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
- TDP-43 immunoreactivity was detected in the hypoglossal nucleus in all cases of amyotrophic lateral sclerosis, all cases of frontotemporal lobar degeneration and some of cases of primary lateral sclerosis (PLS).
- There is no evidence, that common variants in TDP-43 confer a strong risk to the development of sporadic FTD.
- TDP-43 has a role in transcription and splicing regulation and may be involved in other cellular processes such as microRNA biogenesis, apoptosis, and cell division [review]
- TDP-43 inclusions seen in frontotemporal dementias and motor neuron diseases are specific to a neurodegenerative process.
- TDP-43 is a neuronal activity-responsive factor functioning in the regulation of neuronal plasticity, the impairment of which leads to frontotemporal lobar degeneration.
- These results suggest that neurons with abnormal TDP-43 immunoreactivities are associated with dysfunction of the secretory pathway in motor neurons.
- Sequencing of the TDP-43 gene led to the identification of a novel missense mutation, Ala-315-Thr, which segregates with all affected members of an autosomal dominant motor neuron disease family.
- The discovery of a missense mutation Ala-315-Thr in a family with dominantly inherited motor neuron disease provides a direct link between altered TDP-43 function and neurodegeneration.
- 2E2-D3 monoclonal antibody reacted with human TDP-43, but not mouse or rat TDP-43, and recognized amino acids 205-222 of human TDP-43
- ubiquitin-positive inclusions (FTLD-U) and amyotrophic lateral sclerosis pathogenesis may be linked mechanistically to deleterious perturbations of nuclear trafficking and solubility of TDP-43
- Cdk6 up-regulation in TDP-43-depleted cells is accompanied by an increase in phosphorylation of two of its major targets, the retinoblastoma protein pRb and pRb-related protein pRb2/p130.
- study identified neighboring mutations in a highly conserved region of TARDBP in sporadic and familial amyotrophic lateral sclerosis (ALS) cases; evidence suggests a pathophysiological link between TDP-43 and ALS
- These findings further corroborate that TDP-43 is involved in amyotrophic lateral sclerosis pathogenesis.
- TAR DNA-binding protein 43 immunohistochemistry reveals extensive neuritic pathology in frontotemporal lobar degeneration with ubiquitinated inclusions.
- This study identified two variants in TARDBP, which would encode Gly290Ala and Gly298Ser forms of TDP-43, in two kindreds with familial ALS.
- In three affected individuals in two generations of one family with amyotrophic lateral sclerosis (ALS), a single base-pair change from A to G is found at position 1028 in TDP-43. providing a new insight into the molecular pathogenesis of ALS.
- Mutant variant A90V may be a genetic risk factor for FTLD/ALS because it predisposes nuclear TDP-43 to redistribute to the cytoplasm and form pathological aggregates.
- As a predictive test, plasma TDP-43 level may have great practical value
- These findings provide further insight into the burden and clinical significance of TDP-43 pathology in disorders other than FTLD-U and amyotrophic lateral sclerosis.
- pathogenic structural variants were not observed in the cases and there was no genetic or haplotype association with disease status across the TARDBP locus
- Phosphorylated TDP-43 is a major component of the inclusions, and that abnormal phosphorylation of TDP-43 is a critical step in the pathogenesis of FTLD-U and ALS.
- analysis of mutations in TDP-43 that may have roles in neurodegenerative disorders [review]
- There are many precedents in neurodegenerative disease in which rare single-gene mutations have given great insight into understanding disease processes, which is why the TDP-43 mutations are potentially very important.
- Data show that Caspase-cleaved TDP-43 presents in Hirano bodies, tangles, reactive astrocytes and neuritic plaques of the AD brain and co-localized with ubiquitin labeled neurons as well as dystrophic neurites within plaque regions.
- These results suggest that the phosphorylation of Ser409/410 is an abnormal event in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
- Data do not support a role for TDP-43 in prion disease pathogenesis and argue that TDP-43 inclusions define a distinct group of neurodegenerative disorders.
- TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
- Genetic variability in a miR-659 binding-site of GNR increased the risk for TDP-43 positive frontotemporal dementia.
- Neuropathological examination reveals cytoplasmic deposition of the TDP-43 protein in affected pedigree members with frontotemporal lobar degeneration--motor neuron disease.
- Mutations in TARDBP are a rare cause of familial non-superoxide dismutase-1 amyotrophic lateral sclerosis in two German pedigrees.
- Three missense mutations in exon 6 of TARDBP were identified in the analysis of 92 familial amyotrophic lateral sclerosis patients, while no mutations were detected in 24 patients with sporadic amyotrophic lateral sclerosis .
- Data show that the pathological deposits with antibodies against TDP-43 has involved in the neuropathogenesis of the amyotrophic lateral sclerosis/parkinsonism-dementia complex of Guam.
- Data show that sporadic amyotrophic lateral sclerosis of long duration is associated with relatively mild TDP-43 pathology.
- Presence of TDP-43 is associated with a range of neurodegenerative diseases.
- mutations in the TARDBP gene have an important role in the pathogenesis of amyotrophic lateral sclerosis .
- Morphologically distinct inclusion components may reflect the process of TDP-43 aggregation and interaction with other proteins: determining these latter may contribute towards understanding the pathogenesis of FTLD with TDP-43 proteinopathy.
- Data show that the ALS patients had significantly higher levels of TDP-43 in their CSF than the age-matched controls.
- In all Huntington disease cases studied, TDP-43 was frequently colocalized with huntingtin in dystrophic neurites and various intracellular inclusions, but not in intranuclear inclusions.
- results indicate for the first time a high frequency of concomitant TDP-43 pathology in argyrophilic grain disease (AGD), and suggest that abnormal accumulation of TDP-43 may be involved in the pathological process and disease progression of AGD
- several mutations of the TDP-43 gene were identified as the causative gene of autosomal-dominant familial ALS (review)
- study found TDP-43-positive aggregates not only in sporadic inclusion body myositis but also in other vacuolar myopathies; TDP-43-positive aggregates would seem to be a general phenomenon among the myopathies associated with rimmed vacuoles
- Intracellular localization of TDP-43 and proteasomal function may be involved in inclusion formation and neurodegeneration in TDP-43 proteinopathies.
- data demonstrate that phosphorylation of S409/410 of TDP-43 is a highly consistent feature in pathologic inclusions in the whole spectrum of sporadic and familial forms of TDP-43 proteinopathies.
- The present case illustrates that isolated TAR DNA-binding protein-43 disorders can produce an ALS-Plus syndrome with extrapyramidal features and supranuclear gaze palsy resembling progressive supranuclear palsy.
- results suggest that the morphological and biochemical features of TDP-43 pathology are common between Alzheimer's disease or dementia with Lewy bodies and a frontotemporal lobar degeneration subtype associated with progranulin gene mutations
- Animal modles with mutations in this gene develop pathology similar to amyotrophic lateral sclerosis[REVIEW]
- Here we report an A to G (931 A>G) mutation in exon 6 of TARDBP, resulting in the substitution of methionine by valine at codon 311, in one patient with autosomal dominant FALS.