Alas2 Antibody

1. 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. PMID: 29958424
2. 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. PMID: 27928941
3. We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis PMID: 26854603
4. N150F ALAS variant catalyzes the forward reaction at a mere 1.2-fold faster rate than that of the reverse reaction. PMID: 26511319
5. 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. PMID: 24718052
6. 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. PMID: 24920668
7. 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 PMID: 24509859
8. 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. PMID: 12191993
9. Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts PMID: 12393610
10. mechanism of up-regulation in erythroleukemia cells exposed to hypoxia PMID: 12393745
11. 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. PMID: 16356476
12. 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. PMID: 18780836

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KEGG: mmu:11656

STRING: 10090.ENSMUSP00000066040

UniGene: Mm.302724