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a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented
int-1 (zeige WNT1 ELISA Kits)-GATA (zeige QRSL1 ELISA Kits) site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons.
From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP (zeige PLP1 ELISA Kits)-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations.
data indicate that the X-linked protoporphyria (zeige FECH ELISA Kits) variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS
In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients.
the primary deficiency in ferrochelatase (zeige FECH ELISA Kits) leads to a secondary increase in ALAS2 expression.
The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects.
the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown.
5 families with X-linked sideroblastic anemia had mutations in a GATA (zeige QRSL1 ELISA Kits) transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.
Loss-of-function FECH (zeige FECH ELISA Kits) and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria (zeige FECH ELISA Kits) and x-linked protoporphyria (zeige FECH ELISA Kits) in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria (zeige FECH ELISA Kits).
Xalas2 might be able to synthesize hemoglobin (zeige HBB ELISA Kits) during hematopoiesis and mediate erythrocyte differentiation by regulating hba3 expression in Xenopus laevis
We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis
Light treatments revealed that ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid (ALA) treatment producing a similar amount of protoprophyrin IX.
The rate of ALA release is also controlled by a hysteretic kinetic mechanism (observed as a lag (zeige STMN1 ELISA Kits) in the ALA external aldimine formation progress curve), consistent with conformational changes governing the dissociation of ALA from ALAS.
impaired mitochondrial [Fe-S] cluster biogenesis in Mfrn1 (zeige SLC25A37 ELISA Kits)(gt/gt (zeige FABP6 ELISA Kits)) cells results in elevated IRP1 (zeige ACO1 ELISA Kits) RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation
Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts
Gene expression and enzymatic assays indicate that erythroid 5-aminolevulinic acid synthase (zeige ALAS1 ELISA Kits) (Alas2) is decreased in hem6 animals, suggesting a mechanism that could account for the anemia.
The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified.
5-aminolevulinate synthase 2
, aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia)
, 5-aminolevulinate synthase, erythroid-specific, mitochondrial
, aminolevulinate, delta-, synthase 2
, delta-ALA synthase 2
, 5-aminolevulinic acid synthase 2
, delta-aminolevulinate synthase 2
, 5-aminolevulinate synthase, erythroid-specific, mitochondrial-like
, delta-ALA synthetase
, delta-ALA synthetase 2
, Aminolevulinate synthase 2, delta
, aminolevulinic acid synthase 2, erythroid
, erythroid-specific delta-aminolevulinate synthase ALAS-E
, erythroid aminolevulinate synthase
, erythroid-specific ALAS