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抗Human ALAS2 抗体:
抗Rat (Rattus) ALAS2 抗体:
抗Mouse (Murine) ALAS2 抗体:
Human Monoclonal ALAS2 Primary Antibody for 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 for WB - ABIN2776923
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 for WB - ABIN2777048
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 for 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
we report that the dynamics of ALAS2 active site loop is anti-correlated with the dynamics of the C-terminal tail and that this anti-correlation can represent a molecular basis for the functional and dynamic asymmetry of the ALAS2 homodimer.
report confirms the considerable variability in manifestations among patients with ALAS2 or SLC25A38 (显示 SLC25A38 抗体) mutations and draws attention to differences in the assessment and the monitoring of iron overload and its complications
A novel ALAS2 missense mutation in exon 9 affects the enzymatic activity of ALAS2 by affecting its interaction with the cofactor pyridoxal 5'-phosphate in X-linked sideroblastic anemia.
a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented
int-1 (显示 WNT1 抗体)-GATA (显示 QRSL1 抗体) 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 (显示 PLP1 抗体)-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 (显示 FECH 抗体) 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 (显示 FECH 抗体) 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.
Xalas2 might be able to synthesize hemoglobin (显示 HBB 抗体) during hematopoiesis and mediate erythrocyte differentiation by regulating hba3 expression in Xenopus laevis
we used bioinformatics and computational biology tools to evaluate the role(s) of the C-terminal tail dynamics in the structure and conformational dynamics of the murine ALAS2 homodimer active site loop.
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 (显示 STMN1 抗体) 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 (显示 SLC25A37 抗体)(gt/gt (显示 FABP6 抗体)) cells results in elevated IRP1 (显示 ACO1 抗体) 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 (显示 ALAS1 抗体) (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