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anti-Human ALAS2 Antikörper:
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Human Monoclonal ALAS2 Primary Antibody für ELISA, WB - ABIN559841
Zhang, Shen, Liu, Wang, Zhao, Yu, Zhang: Hypoxic induction of human erythroid-specific ?-aminolevulinate synthase mediated by hypoxia-inducible factor 1. in Biochemistry 2011
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Cow (Bovine) Polyclonal ALAS2 Primary Antibody für WB - ABIN2777048
Chien, Chang, Lee, Su, Wu: Non-genomic immunosuppressive actions of progesterone inhibits PHA-induced alkalinization and activation in T cells. in Journal of cellular biochemistry 2006
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Cow (Bovine) Polyclonal ALAS2 Primary Antibody für WB - ABIN2776923
Lee, Barton, Rao, Acton, Adler, Beutler: Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. in Blood cells, molecules & diseases 2006
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Human Polyclonal ALAS2 Primary Antibody für IHC, IHC (p) - ABIN4279110
Sawicki, Shang, Wu, Chang, Khechaduri, Sato, Kamide, Liu, Naga Prasad, Ardehali: Increased Heme Levels in the Heart Lead to Exacerbated Ischemic Injury. in Journal of the American Heart Association 2015
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 Antikörper)-GATA (zeige QRSL1 Antikörper) 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 Antikörper)-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 Antikörper) 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 Antikörper) 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 Antikörper) transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.
Loss-of-function FECH (zeige FECH Antikörper) and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria (zeige FECH Antikörper) and x-linked protoporphyria (zeige FECH Antikörper) in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria (zeige FECH Antikörper).
Xalas2 might be able to synthesize hemoglobin (zeige HBB Antikörper) 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 Antikörper) 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 Antikörper)(gt/gt (zeige FABP6 Antikörper)) cells results in elevated IRP1 (zeige ACO1 Antikörper) 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 Antikörper) (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