Alternative Name(s):

Short name: PPO

Species: (Organism)

Homo sapiens (Human)

Gene Names:

PPOX

Tag info:

N-terminal 6xHis-SUMO-tagged

Target Protein AA Sequence:

MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS

Expression Region:

1-477aa

Subcellular Location:

Mitochondrion inner membrane, Peripheral membrane protein, Intermembrane side

Tissue Specificity:

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Protein Length:

Full Length

Pathway:

Mol. Weight:

66.8 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Metabolism

Function:

Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.

Involvement in disease:

Variegate porphyria (VP)

Relevance:

Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Protoporphyrinogen oxidase family

Reference:

"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."Nishimura K., Taketani S., Inokuchi H.J. Biol. Chem. 270:8076-8080(1995)