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Validated All-in-One™ qPCR Primer for GLA(NM_000169.2) Search again
Product ID:
HQP007574
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
GALA
Gene Description:
galactosidase alpha
Target Gene Accession:
NM_000169.2(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 a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties. [provided by RefSeq].
Gene References into function
- novel mutations in patients of European origin with Fabry disease
- Missense mutation (1280A to G, N34S) was detected in exon 1 of alpha-galactosidase gene.
- Alternative splicing in the alpha-galactosidase A gene: increased exon inclusion results in the Fabry cardiac phenotype.
- Overexpression of human alpha-galactosidase A did not affect cellular morphology, which indicates that its overexpression in gene therapy endeavors should be safe.
- Review. Alpha-galactosidase-A deficiency causes Fabry disease, transmitted as an X-linked recessive trait. As the gene shows various mutations, the establishment of phenotype-genotype correlations is limited.
- Review. The GLA gene has been cloned and more than 200 mutations have been identified.
- The adeno-associated virus (AAV) vector containing the alpha-gal A gene was injected into the right quadriceps muscles of Fabry knockout mice.
- Occurrence of edited alpha-gal A transcripts in humans
- Fifteen novel GLA mutations were identified in 22 Spanish Fabry disease patients.
- A previously unreported deletion mutation (c.1072_1074delGAG) in exon 7 of alpha-Gal A gene on Xq22 in a Taiwanese family with Fabry disease is reported.
- 2 new intronic polymorphisms, c.640-16A>G and c.1000-22C>T, were detected with frequencies of 0.14 and 0.25 in both normal individuals and Fabry patients, respectively.
- analysis of mutations in the GLA gene in 121 patients with Fabry disease
- Data show the usefulness of 1-deoxygalactonojirimycin for correction of the lysosomal storage in Fabry fibroblasts harboring different alpha-galactosidase A mutations with residual enzyme activity.
- Studies further define the molecular heterogeneity of the alpha-Gal A mutations in classical Fabry disease, permit precise heterozygote detection and prenatal diagnosis.
- DNA analysis of the alpha-galactosidase A gene confirmed the diagnosis of Fabry disease, showing a de novo point mutation at position 691 of exon 5.
- results indicate that a large proportion of mutant GLA enzymes in Fabry disease patients with residual enzyme activity are kinetically active
- Because of lack of functionality of rescued mutant alpha-galactosidase A, 4-phenylbutyrate seems to be of limited use as a chemical chaperone for Fabry disease.
- There is a significant correlation between the types of mutations of GLA and total Gb3 excretion in Fabry patients.
- 62 Fabry patients in Japan were examined and 24 GLA mutations were found, including 11 novel ones.
- The negative effect of antibody formation in Fabry disease could be overcome by increasing the dose of enzyme administered to mice.
- Two novel different deletions were detected using MLPA assay on two Fabry patients.
- Structural characterization of mutant alpha-galactosidases causing Fabry disease.
- Mutated alpha-galactosidase A did not respond to a pharmacological chaperone
- We report here a new mutation in Fabry disease. The hemizygote did not show corneal manifestations as opposed to heterozygotes in the described family.
- Novel disease-causing mutations were found in 15 unrelated Hungarian families diagnosed with Fabry disease.