Browse our anti-ALAS2 (ALAS2) Antibodies

Full name:
anti-Aminolevulinate, delta-, Synthase 2 Antibodies (ALAS2)
On are 71 Aminolevulinate, delta-, Synthase 2 (ALAS2) Antibodies from 15 different suppliers available. Additionally we are shipping ALAS2 Proteins (5) and ALAS2 Kits (1) and many more products for this protein. A total of 83 ALAS2 products are currently listed.
ALAS, Alas-2, alas-e, ALASE, ANH1, ASB, cb1063, sau, sauternes, XLDPP, XLEPP, XLSA
list all antibodies Gene Name GeneID UniProt
ALAS2 212 P22557
ALAS2 25748 Q63147
ALAS2 11656 P08680

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anti-Human ALAS2 Antibodies:

anti-Rat (Rattus) ALAS2 Antibodies:

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Top referenced anti-ALAS2 Antibodies

  1. Human Monoclonal ALAS2 Primary Antibody for ELISA, WB - ABIN559841 : Zhang, Shen, Liu, Wang, Zhao, Yu, Zhang: Hypoxic induction of human erythroid-specific ?-aminolevulinate synthase mediated by hypoxia-inducible factor 1. in Biochemistry 2011 (PubMed)
    Show all 2 references for 559841

  2. Cow (Bovine) Polyclonal ALAS2 Primary Antibody for WB - ABIN2777048 : Chien, Chang, Lee, Su, Wu: Non-genomic immunosuppressive actions of progesterone inhibits PHA-induced alkalinization and activation in T cells. in Journal of cellular biochemistry 2006 (PubMed)
    Show all 2 references for 2777048

  3. Cow (Bovine) Polyclonal ALAS2 Primary Antibody for WB - ABIN2776924 : Lee, Barton, Rao, Acton, Adler, Beutler: Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. in Blood cells, molecules & diseases 2006 (PubMed)
    Show all 2 references for 2776924

  4. Human Polyclonal ALAS2 Primary Antibody for IHC, IHC (p) - ABIN4279110 : Sawicki, Shang, Wu, Chang, Khechaduri, Sato, Kamide, Liu, Naga Prasad, Ardehali: Increased Heme Levels in the Heart Lead to Exacerbated Ischemic Injury. in Journal of the American Heart Association 2015 (PubMed)

  5. Cow (Bovine) Polyclonal ALAS2 Primary Antibody for IHC, WB - ABIN2777049 : Astner, Schulze, van den Heuvel, Jahn, Schubert, Heinz: Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. in The EMBO journal 2005 (PubMed)

More Antibodies against ALAS2 Interaction Partners

Human Aminolevulinate, delta-, Synthase 2 (ALAS2) interaction partners

  1. int-1 (show WNT1 Antibodies)-GATA (show QRSL1 Antibodies) site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons.

  2. From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP (show PLP1 Antibodies)-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations.

  3. data indicate that the X-linked protoporphyria (show FECH Antibodies) variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS

  4. In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients.

  5. the primary deficiency in ferrochelatase (show FECH Antibodies) leads to a secondary increase in ALAS2 expression.

  6. The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects.

  7. the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown.

  8. 5 families with X-linked sideroblastic anemia had mutations in a GATA (show QRSL1 Antibodies) transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.

  9. Loss-of-function FECH (show FECH Antibodies) and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria (show FECH Antibodies) and x-linked protoporphyria (show FECH Antibodies) in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria (show FECH Antibodies).

  10. ALAS2 gain-of-function mutations increas the specific activity (DeltaAT, DeltaAGTG and p.Q548X) or stability (DeltaG) of the enzyme, thereby leading to the increased erythroid protoporphyrin accumulation causing X-linked protoporphyria (show FECH Antibodies).

Xenopus laevis Aminolevulinate, delta-, Synthase 2 (ALAS2) interaction partners

  1. Xalas2 might be able to synthesize hemoglobin (show HBB Antibodies) during hematopoiesis and mediate erythrocyte differentiation by regulating hba3 expression in Xenopus laevis

Mouse (Murine) Aminolevulinate, delta-, Synthase 2 (ALAS2) interaction partners

  1. We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis

  2. 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.

  3. The rate of ALA release is also controlled by a hysteretic kinetic mechanism (observed as a lag (show STMN1 Antibodies) in the ALA external aldimine formation progress curve), consistent with conformational changes governing the dissociation of ALA from ALAS.

  4. impaired mitochondrial [Fe-S] cluster biogenesis in Mfrn1 (show SLC25A37 Antibodies)(gt/gt (show FABP6 Antibodies)) cells results in elevated IRP1 (show ACO1 Antibodies) RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation

  5. Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts

  6. Gene expression and enzymatic assays indicate that erythroid 5-aminolevulinic acid synthase (show ALAS1 Antibodies) (Alas2) is decreased in hem6 animals, suggesting a mechanism that could account for the anemia.

ALAS2 Antigen Profile

Antigen Summary

The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified.

Alternative names and synonyms associated with ALAS2

  • aminolevulinate, delta-, synthase 2 (alas2) antibody
  • aminolevulinate, delta-, synthase 2 (ALAS2) antibody
  • aminolevulinate, delta-, synthase 2 (Alas2) antibody
  • aminolevulinate, delta-, synthetase 2 (alas2) antibody
  • aminolevulinic acid synthase 2, erythroid (Alas2) antibody
  • ALAS antibody
  • Alas-2 antibody
  • alas-e antibody
  • ALASE antibody
  • ANH1 antibody
  • ASB antibody
  • cb1063 antibody
  • sau antibody
  • sauternes antibody
  • XLDPP antibody
  • XLEPP antibody
  • XLSA antibody

Protein level used designations for ALAS2

5-aminolevulinate synthase 2 , aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) , 5-aminolevulinate synthase, erythroid-specific, mitochondrial , aminolevulinate, delta-, synthase 2 , ALAS-E , delta-ALA synthase 2 , 5-aminolevulinic acid synthase 2 , delta-aminolevulinate synthase 2 , 5-aminolevulinate synthase, erythroid-specific, mitochondrial-like , delta-ALA synthetase , delta-ALA synthetase 2 , Aminolevulinate synthase 2, delta , aminolevulinic acid synthase 2, erythroid , erythroid-specific delta-aminolevulinate synthase ALAS-E , erythroid aminolevulinate synthase , erythroid-specific ALAS

448773 Xenopus (Silurana) tropicalis
473626 Pan troglodytes
704727 Macaca mulatta
100060580 Equus caballus
100174709 Pongo abelii
100410919 Callithrix jacchus
100606858 Nomascus leucogenys
212 Homo sapiens
511791 Bos taurus
25748 Rattus norvegicus
447323 Xenopus laevis
491498 Canis lupus familiaris
64607 Danio rerio
11656 Mus musculus
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