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DSPP encodes two principal proteins of the dentin extracellular matrix of the tooth. Additionally we are shipping Dentin Sialophosphoprotein Kits (26) and Dentin Sialophosphoprotein Antibodies (10) and many more products for this protein.
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no significant dentin malformation was observed in Mep1b (show MEP1B Proteins) (-/-) or Mep1a (show MEP1A Proteins) (-/-) deficient mice.
overexpressing DPP inhibited skeletal development, suggesting that the balanced actions between the NH2- and COOH-terminal fragments of DSPP may be required for normal skeletal development.
Klf10 is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 (show DMP1 Proteins) and Dspp transcription.
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.
This study expands the spectrum of DSPP variants, highlighting their associated phenotypic continuum.
These data indicate that secretome derived from salivary gland cancer cells can influence the expression of two potential biomarkers of oral cancer-namely, bone sialoprotein (show CRISP1 Proteins) (BSP (show KLK6 Proteins)) and dentin sialoprotein (DSP)-in normal salivary gland cells.
DSPP-MMP20 (show MMP20 Proteins) pair may play a role in the normal turnover of cell surface proteins and/or repair of pericellular matrix proteins of the basement membranes in the metabolically active duct epithelial system of the nephrons.
BMP2 (show BMP2 Proteins) and RUNX2 (show RUNX2 Proteins) are expressed exclusively by osteoblasts whereas DSPP and LOXL2 (show LOXL2 Proteins) are expressed exclusively by odontoblasts. (Review)
A novel pathogenic splicing-mutation c.52-1G>A of DSPP is associated with dentinogenesis imperfecta shields type II.
expression of MMP-20 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
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 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