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anti-Human ALAS1 Antikörper:
anti-Mouse (Murine) ALAS1 Antikörper:
anti-Rat (Rattus) ALAS1 Antikörper:
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Human Polyclonal ALAS1 Primary Antibody für IHC (p), SimWes - ABIN252387
Zheng, Shan, Lambrecht, Donohue, Bonkovsky: Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin. in Molecular and cellular biochemistry 2008
Show all 3 Pubmed References
Human Monoclonal ALAS1 Primary Antibody für ELISA, WB - ABIN559839
Leick, Wojtaszewski, Johansen, Kiilerich, Comes, Hellsten, Hidalgo, Pilegaard: PGC-1alpha is not mandatory for exercise- and training-induced adaptive gene responses in mouse skeletal muscle. in American journal of physiology. Endocrinology and metabolism 2008
the heme-binding site in the N-terminal region of the mature ALAS1 protein is also necessary for the heme-dependent oxidation of ALAS1.
ALAS1 mRNA and activity were elevated approximately ~3- and 5-fold, and HMB synthase activity was approximately half-normal (~42%)
These results indicate that ALAS1 is a novel NR5A-target gene and participates in steroid hormone production.
Lon (zeige LONP1 Antikörper) peptidase 1 (zeige CNDP2 Antikörper) (LONP1 (zeige LONP1 Antikörper))-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells.
REVIEW: mechanisms involving ALAS deficiency, point mutations, post translational processing, and complex formation with succinyl CoA (zeige OXCT1 Antikörper) synthetase subunit B in the pathogenesis of hereditary sideroblastic anemia.
ALAS expression is regulated by AP-1 (zeige FOSB Antikörper) complex through sequestration of cAMP-response element protein (CRE)-binding protein (CBP (zeige CREBBP Antikörper)) coactivator in human cells
ALAS gene expression is regulated by Hepatic nuclear factor 3 and nuclear factor 1
First described frameshift ALAS2 (zeige ALAS2 Antikörper) mutation, CD506-507 (-C).
in the liver of Acute liver failure patients, there may be an increase in free heme concentration which down-regulating ALAS1 gene expression
Alternative splicing of human ALAS1 generates two mRNAs with different 5'-UTRs: a major one, where exon 1B is omitted, and a minor form containing exon 1B.
RNAi-mediated silencing of hepatic Alas1 effectively prevents and treats the induced acute attacks in acute intermittent porphyria mice.
Both ALAS1 mRNA and protein content were induced in diabetic animals, accompanied by decreased Akt (zeige AKT1 Antikörper) phosphorylation and increased nuclear FOXO1 (zeige FOXO1 Antikörper), PGC-1alpha (zeige PPARGC1A Antikörper) and FOXO1 (zeige FOXO1 Antikörper)-PGC-1alpha (zeige PPARGC1A Antikörper) complex levels.
Egr-1 (zeige EGR1 Antikörper) regulates the transcriptional repression of mouse delta-aminolevulinic acid synthase 1 by heme
Mice bearing a homozygous knock-in allele were lethal by embryonic day 8.5, demonstrating that ALAS-N is essential for early embryogenesis.
Ser (zeige SIGLEC1 Antikörper)-254 is critical for formation of a competent catalytic complex by coupling succinyl-CoA (zeige OXCT1 Antikörper) binding to enzyme conformational equilibria
identified a drug-responsive enhancer in the ALAS1 gene
Histidine-282 impacts a variety of ALAS functions, including substrate and pyridoxal 5'-phosphate (PLP (zeige C3 Antikörper))-binding and catalysis.
The findings show that a B2 SINE retrotransposon can contribute to the regulation of ALAS1 and SINEs in 5'-UTR (zeige UTS2R Antikörper) regions contribute to inter-individual differences in gene expression.
This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. The enzyme encoded by this gene is the housekeeping enzyme\; a separate gene encodes a form of the enzyme that is specific for erythroid tissue. The level of the mature encoded protein is regulated by heme: high levels of heme down-regulate the mature enzyme in mitochondria while low heme levels up-regulate. A pseudogene of this gene is located on chromosome 12. Multiple alternatively spliced variants, encoding the same protein, have been identified.
5-aminolevulinate synthase, nonspecific, mitochondrial
, 5-aminolevulinic acid synthase 1
, delta-ALA synthase 1
, delta-aminolevulinate synthase 1
, migration-inducing protein 4
, aminolevulinate synthase H
, succinyl-CoA: glycine C-succinyl transferase
, 5-aminolevulinate synthase 1
, aminolevulinic acid synthase 1
, delta-ALA synthetase
, aminolevulinate, delta, synthase 1
, delta-ALA synthetase 1
, aminolevulinate, delta-, synthase 1
, Delta-ALA synthetase
, 5-aminolevulinate synthase, nonspecific, mitochondrial-like
, 5-aminolevulinic acid synthase
, alanyl-tRNA synthetase protein
, aminolevulinate synthase 1