Analytical Data
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Gene name
PMPCB
- Application
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Alternative Names
PMPCB；MPPB；Mitochondrial-processing peptidase subunit beta
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75439
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Expression Region
44-489aa
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AA Sequence
STQAATQVVLNVPETRVTCLESGLRVASEDSGLSTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVSHDELLDLAKFHFGDSLCTHKGEIPALPPCKFTGSEIRVRDDKMPLAHLAIAVEAVGWAHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCESSTVADMLHVVQKEWMRLCTSVTESEVARARNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVNAETIREVCTKYIYNRSPAIAAVGPIKQLPDFKQIRSNMCWLRD
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Molecular Weight
55.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
PMPCB (Precursor Metaloprotease B) is a vital enzyme implicated in the processing of precursor proteins within mitochondria, playing a crucial role in cellular energy metabolism and mitochondrial protein maturation. This enzyme is part of a larger family of metalloproteases, which are known for their ability to cleave peptide bonds in the presence of metal ions, facilitating various biological processes. Research on PMPCB has gained traction due to its significance in understanding mitochondrial function and its potential links to various diseases, including neurodegenerative disorders and metabolic syndromes. The study of PMPCB involves exploring its structure, substrate specificity, and regulatory mechanisms, which can unveil insights into mitochondrial dynamics. Furthermore, its role in the assembly of essential mitochondrial proteins underscores its importance in cellular health, prompting investigations into its therapeutic potential. Given the increasing prevalence of mitochondrial disorders, characterizing PMPCB and its interactions could provide novel strategies for drug development and interventions aimed at enhancing mitochondrial function. Overall, research on PMPCB not only contributes to our fundamental understanding of mitochondrial biology but also opens pathways for innovative approaches in treating mitochondrial-related diseases.
