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Fibrillar collagen types I-III are synthesized as precursor molecules known as procollagens. Zusätzlich bieten wir Ihnen PCOLCE Antikörper (66) und PCOLCE Proteine (12) und viele weitere Produktgruppen zu diesem Protein an.
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Human PCOLCE ELISA Kit für Sandwich ELISA - ABIN414619
Malaud, Merle, Piquer, Molina, Salvetat, Rubrecht, Dupaty, Galea, Cobo, Blanc, Saussine, Marty-Ané, Albat, Meilhac, Rieunier, Pouzet, Molina, Laune, Fareh: Local carotid atherosclerotic plaque proteins for the identification of circulating biomarkers in coronary patients. in Atherosclerosis 2014
Show all 2 Pubmed References
Rat (Rattus) PCOLCE ELISA Kit für Sandwich ELISA - ABIN847993
Ippolito, AbdulHameed, Tawa, Baer, Permenter, McDyre, Dennis, Boyle, Hobbs, Streicker, Snowden, Lewis, Wallqvist, Stallings: Gene expression patterns associated with histopathology in toxic liver fibrosis. in Toxicological sciences : an official journal of the Society of Toxicology 2015
Results suggest that PCPE-1 binding to syndecans and/or fibronectin (zeige FN1 ELISA Kits) may control collagen fibril assembly on the cell surface.
The analysis of the PCPE-1 interaction network based on Gene Ontology terms suggests that, besides its role in collagen deposition, PCPE-1 might be involved in tumour growth, neurodegenerative diseases and angiogenesis.
The results of this study suggested that nuclear entrapment of PCOLCE and its extracellular depletion represents a novel molecular mechanism in late-onset muscle fibrosis.
Procollagen C-proteinase (zeige BMP1 ELISA Kits) enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.
data generated by our system, support our hypothesis that combined data on PCPE concentration and isoforms may be useful for the diagnosis and follow-up of bone diseases
Procollagen C-proteinase (zeige BMP1 ELISA Kits) enhancer stimulates procollagen processing by binding to the C-propeptide region only.
procollagen C-proteinase enhancer-1 (PCPE-1) binds to heparin/heparan sulfate (zeige GLCE ELISA Kits) and has a role in interaction with cells
Role of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.
Data show that only those containing both PCPE1 CUB1 and CUB2 were capable of enhancing BMP-1 (zeige BMP1 ELISA Kits) activity and binding to a mini-procollagen substrate with nanomolar affinity.
PCPE binds to sites on either side of the procollagen cleavage site, thereby facilitating the action of procollagen C-proteinases.
Bone morphogenetic protein-1/mTLD and PCPE-1 are upregulated in corneal scars. Both proteins may therefore contribute to the process of corneal scarring.
PCPE1 and PCPE2 (zeige PCOLCE2 ELISA Kits) were found to be collagen-binding proteins, capable of binding at multiple sites on the triple helical portions of fibrillar collagens and also capable of competing for such binding with procollagen C-proteinases
Fibrillar collagen types I-III are synthesized as precursor molecules known as procollagens. These precursors contain amino- and carboxyl-terminal peptide extensions known as N- and C-propeptides, respectively, which are cleaved, upon secretion of procollagen from the cell, to yield the mature triple helical, highly structured fibrils. This gene encodes a glycoprotein which binds and drives the enzymatic cleavage of type I procollagen and heightens C-proteinase activity.
procollagen C-endopeptidase enhancer 1
, procollagen C-proteinase enhancer 1
, procollagen COOH-terminal proteinase enhancer 1
, procollagen, type 1, COOH-terminal proteinase enhancer
, type 1 procollagen C-proteinase enhancer protein
, type I procollagen COOH-terminal proteinase enhancer
, procollagen C-endopeptidase enhancer protein
, procollagen C-proteinase enhancer protein
, astroglial cell transcript 2