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DSPP encodes two principal proteins of the dentin extracellular matrix of the tooth.
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Human DSPP ELISA Kit für Sandwich ELISA - ABIN813771
Ozeki, Mogi, Yamaguchi, Hiyama, Kawai, Hase, Nakata, Nakamura, Kramer: Differentiation of human skeletal muscle stem cells into odontoblasts is dependent on induction of ?1 integrin expression. in The Journal of biological chemistry 2014
Human DSPP ELISA Kit für Sandwich ELISA - ABIN415298
Rody, Wijegunasinghe, Holliday, McHugh, Wallet: Immunoassay analysis of proteins in gingival crevicular fluid samples from resorbing teeth. in The Angle orthodontist 2016
Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (zeige ASIP ELISA Kits) (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP (zeige DSP ELISA Kits) 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 (zeige CRISP1 ELISA Kits) (BSP (zeige KLK6 ELISA Kits)) and dentin sialoprotein (DSP)-in normal salivary gland cells.
DSPP-MMP20 (zeige MMP20 ELISA Kits) 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 (zeige BMP2 ELISA Kits) and RUNX2 (zeige RUNX2 ELISA Kits) are expressed exclusively by osteoblasts whereas DSPP and LOXL2 (zeige LOXL2 ELISA Kits) 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 (zeige DMP1 ELISA Kits) 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.
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 (zeige Vcan ELISA Kits)
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 (zeige MMP2 ELISA Kits) 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
Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (zeige C3 ELISA Kits) (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP (zeige DSP ELISA Kits) 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 (zeige DMP1 ELISA Kits)-null mice and suggest that DSPP and DMP1 (zeige DMP1 ELISA Kits) 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 (zeige MEP1B ELISA Kits) (-/-) or Mep1a (zeige MEP1A ELISA Kits) (-/-) 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 (zeige KLF10 ELISA Kits) is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 (zeige DMP1 ELISA Kits) and Dspp transcription.
DMOG can enhance Dspp expression through VEGF (zeige VEGFA ELISA Kits)-induced stabilization of Runx2 (zeige RUNX2 ELISA Kits) 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.
The results showed that the concentrations of F ion in F and F+Al groups were increased significantly. F induced the mottled (zeige ATP7A ELISA Kits) 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