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anti-Human DMP1 Antikörper:
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dentin matrix protein 1 was detected in the periodontal ligament co-localized with periostin (zeige POSTN Antikörper) in the vicinity of the cement
The Dentin matrix protein1 (Dmp1) is an acidic phosphoprotein of osteocytes proposed to participate in bone and dentin mineralization.
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 (zeige DNMT1 Antikörper) 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 (zeige MDM2 Antikörper)-p53 (zeige TP53 Antikörper) pathway
Expressions of dentin matrix protein (DMP)-1 and osteopontin (OPN (zeige SPP1 Antikörper)) were observed in both normal dentin and dentin from DGI (zeige DSG1 Antikörper)-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.
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 (zeige DSPP Antikörper) on apoptosis of the cells.
Findings support the critical role of DMP1 in maintaining the integrity of the auditory ossicles and its bony membrane
Results show that transgenic expression of Dspp (zeige DSPP Antikörper) partially rescued the long bone defects of Dmp1-null mice and suggest that DSPP (zeige DSPP Antikörper) 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 (zeige NES Antikörper)(+) 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 (zeige NES Antikörper)(+) cells and bone formation.
mutation creates a lower set point for extracellular phosphate and maintains it through the regulation of Fgf23 (zeige FGF23 Antikörper) cleavage and expression
Data show that the phenotype of Notch (zeige NOTCH1 Antikörper) activation in osteocytes was prevented in matrix protein 1 (Dmp1)-Cre;Rosa(Notch (zeige NOTCH1 Antikörper)) mice hemizygous for the Dmp1-sclerostin (SOST (zeige SOST Antikörper)) transgene.
Klf10 (zeige KLF10 Antikörper) is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 and Dspp (zeige DSPP Antikörper) 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 (zeige Vcan Antikörper) 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.
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