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DSPP encodes two principal proteins of the dentin extracellular matrix of the tooth. Additionally we are shipping Dentin Sialophosphoprotein Kits (31) and Dentin Sialophosphoprotein Proteins (9) and many more products for this protein.
Showing 10 out of 14 products:
Human Polyclonal DSPP Primary Antibody for IHC (p) - ABIN2559412
Zhan, Liu, Wang: The Role of MicroRNA-143-5p in the Differentiation of Dental Pulp Stem Cells into Odontoblasts by Targeting Runx2 via the OPG/RANKL Signaling Pathway. in Journal of cellular biochemistry 2017
The levels of DSPP silencing-induced downregulation differed amongst CSC markers, with ABCG2 and CD44 (show CD44 Antibodies) showing more pronounced downregulations.
the transgenic expression of DPP significantly improved the dentin defects in Dspp-null mice. These data provide in vivo evidence that DPP may promote the deposition of hydroxyapatite crystals during the formation and mineralization of dentin, which is in agreement with the in vitro findings described in earlier reports.
Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (show ASIP Antibodies) (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP (show DSP Antibodies) domain regulates DSPP expression and odontoblast homeostasis via a positive feedback loop.
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 Antibodies) (BSP (show KLK6 Antibodies)) and dentin sialoprotein (DSP)-in normal salivary gland cells.
DSPP-MMP20 (show MMP20 Antibodies) 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 Antibodies) and RUNX2 (show RUNX2 Antibodies) are expressed exclusively by osteoblasts whereas DSPP and LOXL2 (show LOXL2 Antibodies) 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
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 Antibodies)
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 Antibodies) 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
our findings demonstrate that MMP9 (show MMP9 Antibodies) is important for tooth development and DSP (show DSP Antibodies) is a novel target of MMP9 (show MMP9 Antibodies) during dentinogenesis.
The C-terminal DSP domain induced phosphorylation of occludin Ser(490) and focal adhesion kinase (FAK) Ser(722) and Tyr(576). Coexpression of DSP, occludin and FAK was detected in dental mesenchymal cells during tooth development. Occludin physically interacts with FAK, and occludin and FAK phosphorylation can be blocked by DSP and occludin antibodies.
stable Hey1overexpressing cells expressed higher levels of dentin sialophosphoprotein (DSPP) and exhibited higher mineralization capabilities following stimulation by differentiation medium. Furthermore, RNA interferencemediated knockdown of Hey1 (show HEY1 Antibodies) downregulated the expression levels of DSPP in OLCs stimulated by differentiation medium.
Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (show C3 Antibodies) (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP (show DSP Antibodies) domain regulates DSPP expression and odontoblast homeostasis via a positive feedback loop.
Results show that transgenic expression of Dspp partially rescued the long bone defects of Dmp1 (show DMP1 Antibodies)-null mice and suggest that DSPP and DMP1 (show DMP1 Antibodies) may function synergistically within the complex milieu of bone matrices.
Data show provide evidence that DSPP is important for normal mineralization of both dentin and enamel.
no significant dentin malformation was observed in Mep1b (show MEP1B Antibodies) (-/-) or Mep1a (show MEP1A Antibodies) (-/-) 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 (show KLF10 Antibodies) is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 (show DMP1 Antibodies) and Dspp transcription.
DMOG can enhance Dspp expression through VEGF (show VEGFA Antibodies)-induced stabilization of Runx2 (show RUNX2 Antibodies) protein.
The results showed that the concentrations of F ion in F and F+Al groups were increased significantly. F induced the mottled (show ATP7A Antibodies) enamel and irregular abrasion of teeth, which might occur as a consequence of depressed DSPP mRNA and DPP protein expression.
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 phosphoprotein
, dentin phosphoryn
, dentin sialoprotein
, Dentin sialoprotein
, Dentine sialoprotein
, dentin sailophosphoprotein
, dentin sialophosphoprotein
, dentin matrix protein 3
, LOW QUALITY PROTEIN: dentin sialophosphoprotein