DMP1
DMP1 (dentin matrix acidic phosphoprotein 1) is an acidic phosphoprotein of bone and tooth tissues that is critical for proper mineralisation of bone and dentin. It acts in the nucleus of undifferentiated osteoblasts and, once phosphorylated, in the extracellular matrix, where it directs mineralised matrix formation. Browse Assay Genie's current range of DMP1 research reagents below, or read on for the biology behind the target.
DMP1 is an extracellular matrix protein with an unusual dual role during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, the unphosphorylated form acts as a transcriptional component that activates osteoblast-specific genes such as osteocalcin. During the transition from osteoblast to osteocyte, DMP1 is phosphorylated and exported into the extracellular matrix, where it regulates the nucleation of hydroxyapatite and orchestrates mineralised matrix formation.
The DMP1 protein contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp (RGD) cell attachment sequence and a DNA binding domain. These features fit its two locations: it can bind DNA in the nucleus and engage cells and mineral in the matrix. It is present in diverse cells of bone and tooth tissues and is a member of the small integrin binding ligand N-linked glycoprotein (SIBLING) family. Its subcellular locations include the nucleus, the cytoplasm and the extracellular matrix.
The DMP1 gene was previously described under the name dentin matrix acidic phosphoprotein. Mutations in the gene are known to cause autosomal recessive hypophosphatemia, a disease that presents as rickets and osteomalacia, which links the protein directly to skeletal mineral homeostasis. The gene structure is conserved in mammals, and a rat ortholog named Dmp1 is recorded. Two transcript variants encoding different isoforms have been described. Researchers studying biomineralisation, osteocyte biology and heritable bone disease use DMP1 as a marker and as a mechanistic entry point.
DMP1 may activate osteoblast-specific genes such as osteocalcin from the nucleus of undifferentiated osteoblasts, making it a useful focus for differentiation studies.
Phosphorylation and export of DMP1 into the matrix marks the osteoblast to osteocyte transition, so it is relevant to tracking that change.
DMP1 regulates hydroxyapatite nucleation and is critical for mineralisation of bone and dentin, supporting research on matrix formation.
Mutations in DMP1 cause autosomal recessive hypophosphatemia with rickets and osteomalacia, giving the gene clear relevance to heritable bone disease research.
DMP1 has a dual function in osteoblast differentiation. Unphosphorylated DMP1 in the nucleus activates osteoblast-specific genes such as osteocalcin. After phosphorylation it is exported to the extracellular matrix, where it regulates hydroxyapatite nucleation and supports mineralised matrix formation in bone and dentin.
The HGNC name is dentin matrix acidic phosphoprotein 1, and the gene was previously named dentin matrix acidic phosphoprotein. No other aliases are listed. Two transcript variants encoding different isoforms have been described, so check which isoform is relevant to your work.
Mutations in DMP1 cause autosomal recessive hypophosphatemia, which manifests as rickets and osteomalacia. The gene structure is conserved in mammals, and a rat ortholog called Dmp1 is recorded. Always check the datasheet of any product for its validated reactivity.
Other SIBLING family members and osteoblast markers relevant to bone and dentin mineralisation research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13316; product specifications from Assay Genie datasheets.