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DSPP encodes two principal proteins of the dentin extracellular matrix of the tooth. Additionally we are shipping Dentin Sialophosphoprotein Kits (36) and Dentin Sialophosphoprotein Antibodies (9) and many more products for this protein.
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DMOG can enhance Dspp expression through VEGF (show VEGFA Proteins)-induced stabilization of Runx2 (show RUNX2 Proteins) protein.
total dentin volume in DSPP KO animals significant changes in the ultrastructural organization exist
the expression of DSPP precursor protein is required for normal odontoblast lineage differentiation
DPP is essential for the formation of well-defined tooth structures with mineralized dentin matrix.
continuous DSPP action is required for the growth and/or maintenance of the mandibular condylar cartilage
Data indicate that that Wnt10a (show WNT10A Proteins) regulates Dspp expression in mesenchymal cells.
Inactivation of DSPP leads to loss of alveolar bone and cementum in PDL of Dspp null mice. loss of DSPP results in periodontal diseases indicates that this molecule plays vital role in maintaining health of periodontium.
DSS (show PMP22 Proteins) domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo.
Results indicate that dentin sialophosphoprotein (DSPP) is a downstream effector molecule that mediates the roles of dentin matrix protein 1 (DMP1 (show DMP1 Proteins)) in dentinogenesis.
In addition to the peptide bond Gly(451)-Asp (show C3 Proteins)(452), there must be a cryptic cleavage site or sites close to Asp (show C3 Proteins)(452) in the mouse DSPP that can be cleaved by BMP1 (show BMP1 Proteins).
A novel pathogenic splicing-mutation c.52-1G>A of DSPP is associated with dentinogenesis imperfecta shields type II.
expression of MMP-20 (show MMP20 Proteins) and co-expression and potential interaction with DSPP in human major salivary gland tissues
mutations of the DSP-PP P4 to P4' cleavage site can block, impair or accelerate dentin sialoprotein phosphophoryn cleavage, and suggest that its Bone morphogenic protein 1 cleavage site is conserved in order to regulate its cleavage efficiency
DMP1 (show DMP1 Proteins) and DSPP were more abundant in carious than in sound samples.
Domain of dentine sialoprotein mediates proliferation and differentiation of human periodontal ligament stem cells.
analysis of a mutation in DSPP causing dentinogenesis imperfecta and characterization of the mutational effect
DSS (show NR0B1 Proteins) domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo.
efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site
A review of hereditary dentine diseases resulting from mutations in DSPP gene suggests that the localization of mutation in the sequence of the DSPP gene might result in a different phenotype due to the diverse cellular fate of the mutated protein.
Data shows all known DSPP mutations (except Y6D) cause nonsyndromic dentin dysplasia,DD-II, and dentinogenesis imperfecta, DGI (show DSG1 Proteins) II & III, by retention of mutant proteins in the endoplasmic reticulum with associated decreased secretion of normal DSPP.
The porcine dentin sialophosphoprotein has an N-terminal domain with at least six N-glycosylations and a C-terminal domain with two glycosaminoglycan attachments and at least two O-glycosylations.
Astacins in the predentin matrix cleave Dspp.
isolation of DSP from pig dentin and demonstration that it is a proteoglycan (show Vcan Proteins)
isolation and characterization of a third domain of DSPP, designated dentin glycoprotein (DGP)
correspondence between DSPP cleavage sites that occur in vivo and those generated in vitro demonstrates that MMP-2 (show MMP2 Proteins) and MMP-20 (show MMP20 Proteins) process DSPP into smaller subunits in the dentin matrix during odontogenesis
DPP length variations are polymorphic and are not associated with dentin defects
porcine DPP-derived arginyl-glycyl-aspartic acid peptide, but not its mutant arginyl-alanyl-aspartic acid peptide, significantly promoted cell migration
This gene encodes two principal proteins of the dentin extracellular matrix of the tooth. The preproprotein is secreted by odontoblasts and cleaved into dentin sialoprotein and dentin phosphoprotein. Dentin phosphoprotein is thought to be involved in the biomineralization process of dentin. Mutations in this gene have been associated with dentinogenesis imperfecta-1\; in some individuals, dentinogenesis imperfecta occurs in combination with an autosomal dominant form of deafness. Allelic differences due to repeat polymorphisms have been found for this gene.
, dentin matrix protein 3
, Dentin sialoprotein
, Dentine sialoprotein
, dentin sailophosphoprotein
, dentin phosphophoryn
, dentin phosphoprotein
, dentin phosphoryn
, dentin sialoprotein