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Validated All-in-One™ qPCR Primer for GFAP(NM_002055.4) Search again
Product ID:
HQP007360
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ALXDRD
Gene Description:
glial fibrillary acidic protein
Target Gene Accession:
NM_002055.4(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
This gene encodes one of the major intermediate filament proteins of mature astrocytes. It is used as a marker to distinguish astrocytes from other glial cells during development.
Gene References into function
- spectrum of GFAP mutations and genotype-phenotype correlation in infantile Alexander disease
- The GFAP gene of a Japanese girl who presented with typical symptoms of Alexander disease but in whom the diagnosis was not proven by histopathology was sequenced. A missense mutation, R239C was identified.
- a new heterozygous amino acid substitution, Val87Gly in exon 1 of GFAP, in palatal myoclonus, pyramidal tract signs, cerebellar signs, marked atrophy of the medulla oblongata and spinal cord, and autosomal dominant inheritance.
- A disease-causing mutation (E362D) has been found in the GFAP protein of a 13-year-old boy with juvenile Alexander disease which characterizes the late-onset, milder form of this disease compared to the severe type.
- interaction with presenilin 1 and 2
- GFAP expression correlates with cytoplasmic expression of wild-type p53 in human primary glioblastoma.
- Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity.
- The first report of identification of the causative mutation of the GFAP gene for neuropathologically proven hereditary adult-onset Alexander's disease suggests a common molecular mechanism underlying the three Alexander's disease subtypes.
- Alternation of arginine residue can give GFAP protein a dominant negative effect, leading to accumulation of GFAP as Rosenthal fibers. Alexander disease novel mutation R79L in Japanese patient.
- significantly elevated in the CSF of neurocysticercosis patients compared with the control
- Novel GFAP splice forms Delta 135 nt, Delta exon 6 and Delta 164 nt were identified. Neuronal GFAP is observed in the hippocampal pyramidal cells of Alzheimer and Down syndrome patients and aged controls, but not hippocampal sclerosis patients.
- A heterozygous T to C transition at nucleotide 1055 of the GFAP gene resulting in an amino acid replacement of leucine by proline at codon 352 (L352P) was noted in an infant with Alexander disease
- A decrease in levels of GFAP in the dorsolateral prefrontal cortex may contribute to the pathophysiology of major depressive disorder, particularly in subjects of relatively young age.
- the GFAPepsilon tail prevents GFAPepsilon homodimerization and homomeric filament formation, whereas the ability to form heterodimers and filaments with GFAPalpha is retained
- Molecular analysis showed that the patient of alexander's disease was a heterozygote of the L331P mutation of GFAP.
- Glial fibrillary acidic protein is reduced in cerebellum of subjects with major depression.
- We present a case that suggests a relationship between mitochondrial abnormality and Alexander disease with GFAP mutation.
- Dominant missense glial fibrillary acidic protein mutations account for nearly all forms of Alexander disease.
- Perinuclear collapse of the intermediate filament GFAP is demonstrated in primary schwannoma cells, which become motile, unspecifically ensheathing the extracellular matrix and forming pseudomesaxons.
- This study found higher levels of GFAP mRNA in white matter and at the pial surface as compared with gray matter levels in all cases of depression, bipolar disorder and schizophrenia.
- A 60% increase in acidic isoforms of GFAP occurred in AD; these isoforms were both phosphorylated and N-glycosylated, while more basic isoforms were O-glycosylated and exhibited no differences between post-mortem AD and control brains.
- Increased GFAP levels in autistic brains signify gliosis, reactive injury, and perturbed neuronal migration processes.
- In a 6-year-old patient with a relatively mild form of Alexander disease, we detected a common R79H mutation in GFAP.
- The genetic analysis revealed a new missense mutation, an A to G transition at nucleotide position 1026 in exon 6, leading to the substitution of glycine for glutamic acid at amino acid position 371(E371G).
- GFAP levels in the CSF were highly elevated in three genetically confirmed cases of Alexander disease clinically conforming with infantile, early and late juvenile forms.
- AP-1 is a key transcription factor that, in part, controls astrocyte-specific expression of genes including the ACT and GFAP genes
- Intravitreal administration of NMDA caused a significant decrease in the thickness of the retinal layers and induced upregulation of glial fibrillary acidic protein (GFAP).
- Data show that glial fibrillary acidic protein-positive progenitor cells give rise to neurons and oligodendrocytes throughout the central nervous system.
- Co-localization, co-immunoprecipitation, and in vitro overlay analyses demonstrated direct interaction of plectin and GFAP.
- These data suggest that the activation of caspases and cleavage of cellular proteins such as GFAP may contribute to astrocyte injury and damage in the Alzheimer's disease brain.
- NFI-X cooperates with (activator protein 1)AP-1 by an unknown mechanism in astrocytes, which results in the expression of a subset of astrocyte-specific genes.
- GFAP was strong expression in both reactive astrocytes and astrocytomas. Expression of both GFAP is more focal in oligodendrogliomas, with staining of mainly intervening astrocytic processes.
- The presence of glial fibrillary acidic protein mutant, R416W, is the characteristic histopathological feature of Alexander disease: a component of Rosenthal fibers.
- Cerebrospinal fluid GFAP levels are of prognostic value in patients with subarachnoid hemorrhage.
- analysis of glial fibrillary acidic protein, metallothionein, and MHC II expression in human, rat and mouse cells
- Isolation of an evolutionary conserved novel GFAP isoform, GFAPkappa, produced by alternative splicing and polyadenylation of the 3'-region of the human GFAP pre-mRNA is described.
- These findings suggest that the functional abnormalities of astrocytes might be induced prior to aggregation of GFAP in Alexander disease and that the functional alteration depends on the location of the domain.
- GFAP was differentially expressed in sclerotic hippocampi compared to non-sclerotic ones.
- A c1178G>T mutation was detected in the GFAP gene of a 35 year old female patient diagnosed with Alexander disease and also in her affected 6 year old son.
- Here we report a case of Alexander disease with occipital predominance and a novel c.799G>C mutation in the GFAP gene.
- GFAP mutations and polymorphisms in 13 unrelated Italian patients affected by Alexander disease.
- An adult form of Alexander disease: a novel mutation(M74T amino acid change) in glial fibrillary acidic protein
- Data suggest a model with the selection of the exon 7a polyadenylation site being the essential and primary event for regulating GFAP alternative processing.
- Novel mutations in exon 6 of the GFAP gene affect a highly conserved if motif in the rod domain 2B and are associated with early onset infantile Alexander disease.
- Here we describe four members of an Italian family affected by adult Alexander disease. Two novel GFAP missense mutations were found involving two very close codons, c.[988C > G, 994G > A], leading to p.[Arg330Gly, Glu332Lys].
- This is the first report of a novel deletion mutation in the glial fibrillary acidic protein gene with a frame shift associated with Alexander disease.
- A novel mutation, Y83H, and a previously reported mutation, R88C, were identified in 3 cases with the infantile or juvenile form of Alexander disease.
- Identification of two GFAP mutations, coupled on a same allele. Functional studies on this allele revealed less severe aggregation patterns compared to those observed with p.R239C GFAP mutant, associated with a severe Alexander disease phenotype.
- Alexander disease mutant GFAP accumulation stimulates autophagy, in a manner regulated by p38 MAPK and mTOR signaling pathways.
- GFAP levels may be used in Guillain-Barre syndrome as a diagnostic marker of the axonal variant and to predict outcome
- Glial fibrillary acidic protein filaments can tolerate the incorporation of assembly-compromised GFAP-delta, but with consequences for filament organization and alphaB-crystallin association
- This protein has been found differentially expressed in the temporal lobe from patients with schizophrenia.
- This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.