Anti-ALAS2 antibody (AA37191)

$187.00


Alternative names 5-aminolevulinate synthase, erythroid-specific, mitochondrial, ALAS-E, EC 2.3.1.37, 5-aminolevulinic acid synthase 2, Delta-ALA synthase 2, Delta-aminolevulinate synthase 2, ALAS2, ALASE, ASB, HEM0_HUMAN, P22557, 212
Source 587?574?
Species Reactivity Human
Applications IF/ICC, IHC, WB
Host Rabbit
Class Polyclonal
Conjugated Unconjugated


Description

Product name Anti-ALAS2 antibody (AA37191)
Catalog number AA37191
Brand family Ango
Product type Primary Antibody
Antibody Alternative Names 5-aminolevulinate synthase, erythroid-specific, mitochondrial antibody, ALAS-E antibody, EC 2.3.1.37 antibody, 5-aminolevulinic acid synthase 2 antibody, Delta-ALA synthase 2 antibody, Delta-aminolevulinate synthase 2 antibody, ALAS2 antibody, ALASE antibody, ASB antibody, HEM0_HUMAN antibody


Biological Information

Immunogen Recombinant protein of human ALAS2
Concentration 1 mg/ml
Isotype IgG
Application Notes WB 1:500 - 1:2000 IHC 1:50 - 1:200 IF 1:10 - 1:100
Purification method Purified by affinity chromatography


Target

Target Name ALAS2
SwissProt ID Link P22557
Subcellular Location Mitochondrion matrix.
Involvement in Disease Anemia, sideroblastic, X-linked: A form of sideroblastic anemia that shows a variable hematologic response to pharmacologic doses of pyridoxine. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. The disease is caused by mutations affecting the gene represented in this entry. Erythropoietic protoporphyria, X-linked dominant: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. XLDPT is characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes, in which a mismatch between protoporphyrin production and the heme requirement of differentiating erythroid cells leads to overproduction of protoporphyrin in amounts sufficient to cause photosensitivity and liver disease. The disease is caused by mutations affecting the gene represented in this entry. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes .
Tissue Specificity Erythroid specific.
Subunit Structure Homodimer. Interacts with SUCLA2.
Sequence Similarities Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.


Poduct Presentation

Form Liquid
Preservative 0.02% (w/v) sodium azide
Storage buffer PBS with 50% glycerol, pH 7.3


Storage and Shipping Information

Storage Store at -20 or -80 C. Avoid multiple freeze/thaw cycles.