Analytical Data
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Gene name
PCOLCE2
- Application
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Alternative Names
PCOLCE2；PCPE2；Procollagen C-endopeptidase enhancer 2
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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
Q9UKZ9
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Expression Region
24-415aa
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AA Sequence
QSPERPVFTCGGILTGESGFIGSEGFPGVYPPNSKCTWKITVPEGKVVVLNFRFIDLESDNLCRYDFVDVYNGHANGQRIGRFCGTFRPGALVSSGNKMMVQMISDANTAGNGFMAMFSAAEPNERGDQYCGGLLDRPSGSFKTPNWPDRDYPAGVTCVWHIVAPKNQLIELKFEKFDVERDNYCRYDYVAVFNGGEVNDARRIGKYCGDSPPAPIVSERNELLIQFLSDLSLTADGFIGHYIFRPKKLPTTTEQPVTTTFPVTTGLKPTVALCQQKCRRTGTLEGNYCSSDFVLAGTVITTITRDGSLHATVSIINIYKEGNLAIQQAGKNMSARLTVVCKQCPLLRRGLNYIIMGQVGEDGRGKIMPNSFIMMFKTKNQKLLDALKNKQC
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Molecular Weight
59.3 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
PCOLCE2 (Procollagen C-endopeptidase enhancer 2) is a critical extracellular matrix protein involved in collagen processing, playing a significant role in tissue remodeling and repair. Research has increasingly focused on its implications in various pathological conditions, including fibrosis, cancer, and cardiovascular diseases. The modulation of collagen maturation and turnover by PCOLCE2 suggests its potential as a therapeutic target or biomarker in diseases characterized by excessive collagen deposition or impaired tissue regeneration. Understanding the molecular mechanisms through which PCOLCE2 enhances procollagen processing could provide insights into extracellular matrix dynamics and open new avenues for the development of interventions aimed at mitigating fibrotic responses or improving wound healing. Recent studies have utilized recombinant PCOLCE2 proteins to investigate their functional roles and interactions with other matrix components, highlighting the importance of this protein in maintaining tissue homeostasis. Given the complexity of extracellular matrix interactions, ongoing research into the biology of PCOLCE2 will likely reveal further insights into its regulatory functions and therapeutic potential, ultimately contributing to improved strategies for managing diseases linked to abnormal collagen metabolism.
