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The product of ALAS2 specifies an erythroid-specific mitochondrially located enzyme. Additionally we are shipping ALAS2 Kits (10) and ALAS2 Proteins (5) and many more products for this protein.
Showing 10 out of 70 products:
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 references for ABIN2777048
Chicken Polyclonal ALAS2 Primary Antibody for WB - ABIN2776924
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 references for ABIN2776924
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 references for ABIN559841
Cow (Bovine) Polyclonal ALAS2 Primary Antibody for IHC, WB - ABIN2777049
Astner, Schulze, van den Heuvel, Jahn, Schubert, Heinz: Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. in The EMBO journal 2005
data indicate that the X-linked protoporphyria (show FECH Antibodies) 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 (show FECH Antibodies) 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 (show QRSL1 Antibodies) transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.
Loss-of-function FECH (show FECH Antibodies) and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria (show FECH Antibodies) and x-linked protoporphyria (show FECH Antibodies) in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria (show FECH Antibodies).
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 (show FECH Antibodies).
A large gain-of-function domain within the C-terminus of ALAS2 is associated with X-linked dominant protoporphyria (show FECH Antibodies).
Late-onset photosensitivity was caused by ALAS2 mutation in a family with dominant protoporphyria (show FECH Antibodies).
Xalas2 might be able to synthesize hemoglobin (show HBB Antibodies) 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 (show STMN1 Antibodies) 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 (show SLC25A37 Antibodies)(gt/gt (show FABP6 Antibodies)) cells results in elevated IRP1 (show ACO1 Antibodies) 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 (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