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DMP1 might be a potential factor contributing to cardiovascular complications in dialysis patients.
DMP1 gene seems to be involved in genetic predisposition to Ankylosing spondylitis (AS).
DMP-1 immunostaining was higher for MTA (show DNMT1 Proteins) and PC, confirming the reparative and bioinductive capacity of these materials.
This review will focus on the aberrant splicing of tumor suppressor/oncogenes that belong to the DMP1-ARF-MDM2 (show MDM2 Proteins)-p53 (show TP53 Proteins) pathway
Expressions of dentin matrix protein (DMP)-1 and osteopontin (OPN (show SPP1 Proteins)) were observed in both normal dentin and dentin from DGI (show DSG1 Proteins)-I affected patients, without significant differences
identify alternative splicing as a mechanism utilized by cancer cells to modulate the DMP1 locus through diminishing DMP1alpha tumour suppressor expression
The findings indicate that DMP-1 is a useful marker of osteogenic differentiation and mineralisation in soft tissue tumours
A family of autosomal recessive form of Hypophosphatemic rickets secondary to a DMP1 mutation located in the first coding exon of the gene, is reported.
Results suggest that FAM20C (show FAM20C Proteins) suppresses FGF23 (show FGF23 Proteins) production by enhancing DMP1 expression, and inactivating mutations in FAM20C (show FAM20C Proteins) cause FGF23 (show FGF23 Proteins)-related hypophosphatemia by decreasing transcription of DMP1.
DMP1 may play an important role in maintaining the chondrogenic phenotype and its possible involvement in altered cartilage matrix remodelling and degradation in disease conditions like osteoarthritis.
phosphorylated DMP1 expressed in marrow stromal cells was an inhibitor of hydroxyapatite formation; the highly phosphorylated C-terminal 57-kDa fragment apparently arising from proteolytic cleavage, like the non-phosphorylated DMP1, was an HA nucleator
This study was designed to investigate the effect of dentin phosphoprotein (show DSPP Proteins) on apoptosis of the cells.
Results show that transgenic expression of Dspp (show DSPP Proteins) partially rescued the long bone defects of Dmp1-null mice and suggest that DSPP (show DSPP Proteins) and DMP1 may function synergistically within the complex milieu of bone matrices.
The collective results indicate that the osteoanabolic response to loading can occur on the periosteal surface when beta-cat levels are significantly reduced in Dmp1-expressing cells.
Nestin (show NES Proteins)(+) cells are one important type of progenitor cell in bone marrow and are associated with bone remodeling. These data indicate that DMP1 plays negative roles in differentiation of Nestin (show NES Proteins)(+) cells and bone formation.
mutation creates a lower set point for extracellular phosphate and maintains it through the regulation of Fgf23 (show FGF23 Proteins) cleavage and expression
Data show that the phenotype of Notch (show NOTCH1 Proteins) activation in osteocytes was prevented in matrix protein 1 (Dmp1)-Cre;Rosa(Notch (show NOTCH1 Proteins)) mice hemizygous for the Dmp1-sclerostin (SOST (show SOST Proteins)) transgene.
Klf10 is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 and Dspp (show DSPP Proteins) transcription.
These findings indicate that glycosylation of DMP1 is a key posttranslational modification process during development and that DMP1-PG functions as an indispensable proteoglycan (show Vcan Proteins) in osteogenesis.
the hypophosphatemia induced osteomalacia phenotype in Dmp1 KO mice is contributed by at least two factors: the low Pi level and the DMP1 local function in mineralization
These results suggest that the LPV motif is essential for the efficient export of secretory DMP1 from the ER to the Golgi complex.
An in situ hybridization study of perlecan, DMP1, and MEPE in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage.
Dentin matrix acidic phosphoprotein is an extracellular matrix protein and a member of the small integrin binding ligand N-linked glycoprotein family. This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. The protein contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation the protein becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in the gene are known to cause autosomal recessive hypophosphatemia, a disease that manifests as rickets and osteomalacia. The gene structure is conserved in mammals. Two transcript variants encoding different isoforms have been described for this gene.
dentin matrix acidic phosphoprotein 1
, dentin matrix protein 1
, serine rich acidic phosphoprotein