Sf9, Insect cells.
Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.
Greater than 95.0% as determined by SDS-PAGE.
PCOLCE produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 433 amino acids (26-449 a.a.) and having a molecular mass of 46.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
PCOLCE is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Recombinant PCOLCE, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 46.6 kDa. The protein consists of 433 amino acids (residues 26-449) and, on SDS-PAGE, exhibits an apparent molecular size of approximately 40-57 kDa.
The recombinant PCOLCE is engineered with a 9 amino acid His tag at the C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
The provided PCOLCE protein solution has a concentration of 0.25 mg/ml and is formulated in a buffer comprising 20mM Tris-HCl (pH 8.0), 10% glycerol, and 0.1M NaCl.
The purity of the PCOLCE protein is determined to be greater than 95.0% using SDS-PAGE analysis.
Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.
Sf9, Insect cells.
ADPQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQDHHH HHH.
Procollagen C-Endopeptidase Enhancer (PCOLCE) is a glycoprotein that plays a crucial role in the maturation of collagen, a primary structural protein in the extracellular matrix of various tissues. The human recombinant form of PCOLCE, produced in Sf9 insect cells, is utilized in research and therapeutic applications to study and enhance collagen processing.
The PCOLCE gene is located on chromosome 7q22.1 and encodes a protein that binds to the C-terminal propeptide of type I procollagen . This binding enhances the activity of procollagen C-proteinase, an enzyme responsible for cleaving the C-terminal propeptides from procollagen molecules, thereby facilitating the formation of mature collagen fibrils .
PCOLCE enhances the enzymatic cleavage of type I procollagen by procollagen C-proteinase. This process is essential for the proper assembly and stabilization of collagen fibrils, which are critical for the structural integrity of connective tissues . The C-terminal processed part of PCOLCE, known as CT-PCPE, may also exhibit metalloproteinase inhibitory activity, further regulating extracellular matrix remodeling .
The recombinant form of PCOLCE is produced using the baculovirus expression system in Sf9 insect cells. This system allows for high-level expression and proper post-translational modifications of the protein, making it suitable for biochemical and structural studies . The human recombinant PCOLCE produced in Sf9 cells retains its functional properties, enabling researchers to investigate its role in collagen maturation and related pathologies.
PCOLCE has significant implications in both clinical and research settings. Its role in collagen maturation makes it a potential target for therapeutic interventions in diseases characterized by abnormal collagen deposition, such as fibrosis and certain connective tissue disorders . Additionally, recombinant PCOLCE is used in various assays to study collagen processing and to develop inhibitors that could modulate its activity for therapeutic purposes .
Mutations or dysregulation of the PCOLCE gene have been linked to several disorders, including Pierpont Syndrome and nonsyndromic sensorineural deafness . Understanding the function and regulation of PCOLCE can provide insights into the pathogenesis of these conditions and aid in the development of targeted therapies.