Recombinant Human DMP-1 Protein (C-6His)

Name: Recombinant Human DMP-1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0678NP
Availability: InStock

BL-0678NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dentin Matrix Protein 1 is produced by our Mammalian expression system and the target gene encoding Leu17-Tyr513 is expressed with a 6His tag at the C-terminus.
Accession	Q13316
Synonym	Dentin Matrix Acidic Phosphoprotein 1; DMP-1; Dentin Matrix Protein 1; DMP1
Gene Background	0
Molecular Mass	55 KDa
Apmol Mass	45-120 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Histidine-HCl, 6% Trehalose, 4% Mannitol, 0.05% Tween 80, pH6.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite.
Subcellular Location	Nucleus. Cytoplasm. Secreted, extracellular space, extracellular matrix. Note=In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus.
Database References	HGNC: 2932 OMIM: 241520 KEGG: hsa:1758 STRING: 9606.ENSP00000340935 UniGene: PMID: 29289709 The Dentin matrix protein1 (Dmp1) is an acidic phosphoprotein of osteocytes proposed to participate in bone and dentin mineralization. PMID: 28247029 Thus, unspDMP-1 is a novel chromatin-enriched RNA that epigenetically regulates cellular proliferation of SQCC. PMID: 29278708 DMP1 might be a potential factor contributing to cardiovascular complications in dialysis patients. PMID: 27390906 DMP1 gene seems to be involved in genetic predisposition to Ankylosing spondylitis (AS). PMID: 26960368 DMP-1 immunostaining was higher for MTA and PC, confirming the reparative and bioinductive capacity of these materials. PMID: 25678029 This review will focus on the aberrant splicing of tumor suppressor/oncogenes that belong to the DMP1-ARF-MDM2-p53 pathway PMID: 26802432 Expressions of dentin matrix protein (DMP)-1 and osteopontin (OPN) were observed in both normal dentin and dentin from DGI-I affected patients, without significant differences PMID: 25578972 identify alternative splicing as a mechanism utilized by cancer cells to modulate the DMP1 locus through diminishing DMP1alpha tumour suppressor expression PMID: 25537728 The findings indicate that DMP-1 is a useful marker of osteogenic differentiation and mineralisation in soft tissue tumours PMID: 25630512 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. PMID: 25180662 Results suggest that FAM20C suppresses FGF23 production by enhancing DMP1 expression, and inactivating mutations in FAM20C cause FGF23-related hypophosphatemia by decreasing transcription of DMP1. PMID: 25026495 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. PMID: 24987156 DMP1 and DSPP were more abundant in carious than in sound samples. PMID: 24441185 DMP-1 is a matrix marker expressed around osteocytes in human woven and lamellar bone and is useful in identifying osteosarcoma and other bone-forming tumours. PMID: 23559304 Mutations in PHEX and DMP1 play a role in causing hypophosphatemic rickets. PMID: 22695891 DMP1 is regulated post-transcriptionally by let-7 during odontoblast differentiation. PMID: 22552299 DMP-1 stimulated production of IL-6/IL-8 from pulp fibroblasts. Inhibition of p38 mitogen-activated protein kinase pathway blocked proinflammatory effect on pulp fibroblasts. DMP-1 might participate in development of inflammatory changes in pulp. PMID: 22152625 Simvastatin plus all-trans retinoic acid reduces expression of WT1 and DMP1 in the promyelocytic leukemia cell line NB4. PMID: 22093791 DMP1 is specifically involved in signaling via extracellular matrix-cell surface interaction. PMID: 21642437 Data show the wide spectrum of genetic variation that can be seen in PHEX, FGF23 and DMP1 when screening a large cohort with hypophosphatemic rickets. PMID: 21050253 after VE-cadherin induction by DMP1, DMP1 inhibited VEGFR-2 phosphorylation and Src-mediated signaling; DMP1 is identified as a new specific inhibitor of VEGF-induced angiogenesis PMID: 21190990 possible role of dentine matrix protein 1 in the aetiology of [aggressive periodontitis] PMID: 21299946 clinical and laboratory observations in this family confirm that DMP1 has an important role in normal skeletal development and mineral homeostasis PMID: 20499351 Study shows the pivotal roles of Dmp1 in HER2/neu-p53 signaling and breast carcinogenesis. PMID: 21062982 study describes a Japanese family that includes 2 autosomal recessive hypophosphatemic rickets-affected siblings carrying a novel mutation of the DMP1 gene (98G>A, W33X), which leads to a truncated DMP protein with no putative biological function PMID: 20213538 The identified genetic mutation underscores the importance of DMP-1 mutations in the pathogenesis of autosomal recessive form of hypophosphatemia. PMID: 19796717 The patterns of expression of FGF-23, MEPE, and DMP1 differ markedly in trabecular bone, suggesting that individual osteocytes may have specialized functions. PMID: 19679205 Three SIBLINGs (small integrin-binding ligand, N-linked glycoproteins) enhance factor H's cofactor activity enabling MCP-like cellular evasion of complement-mediated attack. PMID: 11825898 DMP1 immunostaining intensity and extent scores were significantly higher in adenocarcinoma (p = 0.0004) and squamous carcinoma (p < 0.0001) samples compared with adjacent normal lung tissue PMID: 12929940 dentin matrix protein-1 is processed by Bone morphogenetic protein-1/Tolloid-like proteinases PMID: 14578349 Findings indicate that DMP1 immunohistochemistry is a useful tool for identifying phosphaturic mesenchymal tumors (PMTs). PMID: 15001995 a silencing cis-element may play a critical role in the regulation of DMP1 cell-specific expression PMID: 15108359 8-kb region of the Dentin matrix protein 1 (DMP1) gene is a target for mechanotransduction in osteocytes, and its cis-regulatory activity may be correlated to local strain in bone PMID: 15728181 Dentin matrix protein 1 enhances invasion potential of colon cancer cells by bridging matrix metalloproteinase-9 to integrins and CD44 PMID: 16357164 analysis of a chondroitin sulfate chain attached to the bone dentin matrix protein 1 NH2-terminal fragment PMID: 16421105 DMP1 regulates the expression of the DSPP gene PMID: 16679514 Absence of DMP1 results in defective osteocyte maturation and increased FGF23 expression, leading to pathological changes in bone mineralization. PMID: 17033621 DMP1 may regulate FGF23 expression. PMID: 17033625 DMP1 has a role in breast cancer progression and bone metastases development PMID: 17136477 Thus, our results suggest that Cbfalpha1 upregulates DMP1 gene expression differentially that may contribute to the spatial-temporal expression pattern of DMP1 during odontoblast differentiation. PMID: 17434448 Discussion of DMP1 role in the maturation of odontoblasts and osteoblasts as well as in mineralization; identification of DMP1 mutations in autosomal-recessive hypophosphatemic rickets; and regulation of phosphate homeostasis through FGF23 [review]. PMID: 18037646 mRNA of DMP1 involved in the pathogenesis of hypophosphataemic rickets is highly expressed in cells of the osteoblasts/osteocyte lineage. PMID: 18214537 inactivating mutations in DMP1 increase, through yet unknown mechanisms, FGF23 synthesis and thus enhance renal phosphate excretion--REVIEW PMID: 18660670 binding of DMP1 with GRP-78 receptor might be an important mechanism by which DMP1 is internalized and transported to the nucleus during bone and tooth development PMID: 18757373 Dentin matrix protein-1 isoforms promote differential cell attachment and migration PMID: 18819913 A novel DMP1 deletion is identified as the cause of autosomal recessive hypophosphatemic rickets, as well as demonstrated that the ARHR mutations alter DMP1 cellular processing, and that DMP1 can be regulated by vitamin D. PMID: 19007919 Deletion of mouse Dmp1 results in bone hypomineralization. PMID: 16294270 DMP1 is expressed in salivary gland ducts. PMID: 15329369 DMP1 is expressed in parietal cells of Bowman's capsule and throughout the ductal system of nephrons. PMID: 15954904

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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