ALAS1 Polyklonale Antilichaam, PE-Cy7 Vervoeging

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.

Mitochondrial; nonspecic; 5 aminolevulinate synthase; 5 aminolevulinate synthase nonspecic mitochondrial; 5 aminolevulinic acid synthase; 5-aminolevulinate synthase; 5-aminolevulinic acid synthase 1; Alas 1; ALAS 3; ALAS; ALAS H; ALAS N; ALAS-H; alaS1; ALAS3; ALASH; Aminolevulinate delta synthase 1; Aminolevulinic acid synthase 1; Delta ALA synthetase; Delta aminolevulinate synthase; Delta-ALA synthase 1; Delta-aminolevulinate synthase 1; HEM1_HUMAN; MIG 4; MIG4; Migration inducing protein 4.

211

Human, Mouse, Rat

161-260/640

ALAS1

PE-Cy7

KLH conjugated synthetic peptide derived from human ALAS1/ALAS-H

WB

Purified by Protein A.

488nm/780nm

1µg/µl

WB (1:300-5000)

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

211

Dog, Horse, Rabbit