Recombinant Human Protoporphyrinogen Oxidase (PPOX) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-09425P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Protoporphyrinogen Oxidase (PPOX) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-09425P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Description Recombinant Human Protoporphyrinogen Oxidase (PPOX) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P50336
Target Symbol PPOX
Synonyms MGC8485; PPO; PPOX; PPOX_HUMAN; Protoporphyrinogen oxidase; V290M; Variegate porphyria; VP
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRGIRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSPPFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS
Expression Range 1-477aa
Protein Length Full Length
Mol. Weight 66.8kDa
Research Area Metabolism
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular Location Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Protein Families Protoporphyrinogen oxidase family
Database References

HGNC: 9280

OMIM: 176200

KEGG: hsa:5498

STRING: 9606.ENSP00000343943

UniGene: PMID: 27667166

  • 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 PMID: 25944804
  • 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. PMID: 23601071
  • in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX and HMBS PMID: 25445397
  • 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. PMID: 19656455
  • The mutation 1082-1083insC(1 base pair insertion at position 1082) in exon 10 of the PPOX gene was prevalent in the Swiss population. PMID: 19656457
  • findings emphasize the usefulness of MLPA analysis as a complement to PPOX gene sequencing analysis for comprehensive genetic diagnostics in patients with variegate prophyria PMID: 23324528
  • VP-causing mutation affect the catalytic activity of hPPO by affecting the ability of hPPO to sample the privileged conformations PMID: 23467411
  • 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 PMID: 19229653
  • data deliver further confirmation that the South African and Dutch variegate porphyria families carrying mutation p.R59W shared a common ancestor. PMID: 21910705
  • Forty-seven variegate porphyria-causing mutations were purified by chromatography and kinetically characterized in vitro. PMID: 21048046
  • Two previously undescribed mutations were identified: PPOX1423-1426-delATCT and PPOX2272insG. PMID: 12017191
  • This enzyme in its regular and mutagenized forms is targeted to mitochondria when transfected. PMID: 12556518
  • Information required for targeting to the mitochondria is contained within the first 250 amino acid residues of human PPOX. PMID: 14535846
  • Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using PPOX. PMID: 14669009
  • Protoporphyrinogen oxidase targeting mechanism to the mitochondrion. PMID: 16621625
  • Mutation in protoporphyrinogen oxidase is associated with variegate porphyria PMID: 16947091
  • GATA-1 binding sites in exon 1 constitute key regulatory elements in differential expression of PPOX in erythroid and non-erythroid cells. PMID: 18191920
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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