epitope corresponding to amino acids 61-160 mapping near the N-terminus of ALAS-E of human origin
recommended for detection of precursor and mature ALAS-E of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA; also reactive with additional species, including equine
ALAS-E Background Information 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.
ALAS-E (H-100)
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ALAS-E (H-100): sc-50529. Western blot analysis of ALAS-E expression in mouse heart tissue extract.
