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Human Monoclonal PPOX Primary Antibody for IHC (p), RNAi - ABIN562343
Crooks, Ghosh, Haller, Tong, Rouault: Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery. in Blood 2010
Show all 3 Pubmed References
Cow (Bovine) Polyclonal PPOX Primary Antibody for WB - ABIN2786509
de Vooght, van Wijk, van Solinge: GATA-1 binding sites in exon 1 direct erythroid-specific transcription of PPOX. in Gene 2008
the regulation of PPOX gene expression can also occur through a post-transcriptional modulation of the amount of gene product and this modulation can be mediated by 5' untranslated exon 1.
GAPDH and protoporphyrinogen oxidase were shown to have higher expression in faster growing cell lines and primary tumors. Pharmacologic inhibition of GAPDH or PPOX reduced the growth of colon cancer cells in vitro
Variegate porphyria is the result of decreased protoporphyrinogen oxidase activity. Diet supplementation with vitamins E and C restores PPOX gene expression in lymphocytes of variegate porphyria patients.
in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX and HMBS
The c.851G>T and the c.1013C>G of PPOX gene were found in two and four unrelated families respectively. 1 experienced only photosensitivity, 1 only neurological symptoms and the 2 both clinical manifestations.
The mutation 1082-1083insC(1 base pair insertion at position 1082) in exon 10 of the PPOX gene was prevalent in the Swiss population.
findings emphasize the usefulness of MLPA analysis as a complement to PPOX gene sequencing analysis for comprehensive genetic diagnostics in patients with variegate prophyria
VP-causing mutation affect the catalytic activity of hPPO by affecting the ability of hPPO to sample the privileged conformations
sequenced 27 members of a family with variegate porphyria with a T>A transversion at the intron 6 consensus splicing site in 8 patients and 4 SNPs: c.-414A>C; IVS2+121G>C; c.1188G>A and IVS12+34C>T
data deliver further confirmation that the South African and Dutch variegate porphyria families carrying mutation p.R59W shared a common ancestor.
Forty-seven variegate porphyria-causing mutations were purified by chromatography and kinetically characterized in vitro.
Two previously undescribed mutations were identified: PPOX1423-1426-delATCT and PPOX2272insG.
This enzyme in its regular and mutagenized forms is targeted to mitochondria when transfected.
Information required for targeting to the mitochondria is contained within the first 250 amino acid residues of human PPOX.
Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using PPOX.
Protoporphyrinogen oxidase targeting mechanism to the mitochondrion.
Mutation in protoporphyrinogen oxidase is associated with variegate porphyria
GATA-1 binding sites in exon 1 constitute key regulatory elements in differential expression of PPOX in erythroid and non-erythroid cells.
isolation, characterization and localization of gene.
The tetrapyrrole biosynthetic enzyme PPO1 is required for plastid RNA editing.
determined significant differences in the proteomes of freshly ingested down boli corresponding to the presence or absence of active PPO. These results show that in the presence of PPO the forage protein is less amenable to proteolysis and provide the novel information that the protected proteins are putatively chloroplastically located.
This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. Mutations in this gene cause variegate porphyria, an autosomal dominant disorder of heme metabolism resulting from a deficiency in protoporphyrinogen oxidase, an enzyme located on the inner mitochondrial membrane. Alternatively spliced transcript variants encoding the same protein have been identified.
, protoporphyrinogen oxidase
, Catechol oxidase
, polyphenol oxidase, chloroplastic