Recombinant Human DMP-1

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935106861
info@markelab.com
name
Recombinant Human DMP-1
category
Proteins and Peptides
provider
FineTest
reference
Pr22827
tested applications
Western Blot, ELISA

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Host
Mammalian Cells
Reactivity
Human
Assay Data
Centrifuge the vial at 10000 rpm for 30 s before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg/ml by gently pipetting 2-3 times, don't vortex.
Recommended Dilution
¥
Isotype
¥
Clone ID
¥
Observed MW
45-120 kDa
Expression
Leu17-Tyr513
Purity
Greater than 95% as determined by SDS-PAGE.
Size 1
10μg
Size 2
50μg
Size 3
500μg
Size 4
1mg
Form
Lyophilized powder
Tested Applications
Western Blot, ELISA
Buffer
Lyophilized from a 0.2 μm filtered solution of 20 mM Histidine, 6% Trehalose, 4% Mannitol, 0.05% Tween 80, pH 6.0.
Availability
7 days
Storage
The lyophilized protein is stable at -20°C for up to 1 year. After reconstitution, the protein solution is stable at -20 to -80°C for 3 months or 1 week at 2 to 8°C under sterile conditions. For extended storage, it is recommended to further dilute in working aliquots, avoid repeated freeze/thaw cycle.
UniProt ID
Q13316
Alias
Dentin Matrix Acidic Phosphoprotein 1, DMP-1, Dentin Matrix Protein 1, DMP1
Background
Protein DMP1
Status
RUO
Note
Endotoxin: < 1 EU/µg as determined by LAL test.

Tag : C-terminal His Tag

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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.

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