Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human ALAS2 Antibodies:
anti-Rat (Rattus) ALAS2 Antibodies:
anti-Mouse (Murine) ALAS2 Antibodies:
Go to our pre-filtered search.
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
Show all 2 Pubmed References
Cow (Bovine) Polyclonal ALAS2 Primary Antibody for 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
Show all 2 Pubmed References
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
Cow (Bovine) Polyclonal ALAS2 Primary Antibody for 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
Show all 2 Pubmed References
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 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-GATA 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-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 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 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 transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.
Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria.
ALAS2 gain-of-function mutations increas the specific activity (DeltaAT, DeltaAGTG and p.Q548X) or stability (DeltaG) of the enzyme, thereby leading to the increased erythroid protoporphyrin accumulation causing X-linked protoporphyria.
A large gain-of-function domain within the C-terminus of ALAS2 is associated with X-linked dominant protoporphyria.
Late-onset photosensitivity was caused by ALAS2 mutation in a family with dominant protoporphyria.
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2).
the C-terminal region of ALAS2 protein may function as an intrinsic modifier that suppresses catalytic activity and increases the degradation of its protein, each function of which is enhanced by the Met567Ile mutation and Val562Ala mutation, respectively
Data suggest that ALAS2 gene mutations should be considered not only as causative of X-linked sideroblastic anemia (XLSA) and XLDPP but may also modulate gene function in other erythropoietic disorders.
identification of five probands with sideroblastic anemia and ALAS2 R452S (due to SNP); all were African-American males; all presented with moderate anemia; the four adults presented with iron overload [a multi-case report from the United States]
Xalas2 might be able to synthesize hemoglobin 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.
Data indicate that the 5-aminolevulinate synthase (mALAS2) active site loop harboring the simultaneous seven amino acid mutations was less flexible than the wild type loop.
We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis
N150F ALAS variant catalyzes the forward reaction at a mere 1.2-fold faster rate than that of the reverse reaction.
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 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(gt/gt) cells results in elevated IRP1 RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation
Data suggest the reaction of glycine with ALAS follows a three-step kinetic process, and the substrate 5-aminolevulinate induces a conformational change in ALAS which may modulate product release.
Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts
mechanism of up-regulation in erythroleukemia cells exposed to hypoxia
These findings thus suggest that heme may regulate a wide variety of hitherto unrecognized genes, and further analysis of these genes may clarify their role in erythroid cell differentiation.
Gene expression and enzymatic assays indicate that erythroid 5-aminolevulinic acid synthase (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