protein

Ectonucleotide Pyrophosphatase, Phosphodiesterase 1 (ENPP1, PC1, Plasma Cell Membrane Glycoprotein) (Control Peptide)

MBS653632

0.1 mg

400 USD

Enzyme

Ectonucleotide Pyrophosphatase, Phosphodiesterase 1 (ENPP1, PC1, Plasma Cell Membrane Glycoprotein) (Control Peptide)

[Ectonucleotide Pyrophosphatase, Phosphodiesterase 1]

[ectonucleotide pyrophosphatase/phosphodiesterase family member 1; Ectonucleotide pyrophosphatase/phosphodiesterase family member 1; ectonucleotide pyrophosphatase/phosphodiesterase family member 1; E-NPP 1; Ly-41 antigen; alkaline phosphodiesterase 1; plasma-cell membrane glycoprotein 1; plasma-cell membrane glycoprotein PC-1; membrane component chromosome 6 surface marker 1; phosphodiesterase I/nucleotide pyrophosphatase 1; membrane component, chromosome 6, surface marker 1; ectonucleotide pyrophosphatase/phosphodiesterase 1; Membrane component chromosome 6 surface marker 1; Phosphodiesterase I/nucleotide pyrophosphatase 1; Plasma-cell membrane glycoprotein PC-1]

[ENPP1; ENPP1; M6S1; NPP1; NPPS; PC-1; PCA1; ARHR2; PDNP1; M6S1; NPPS; PC1; PDNP1; E-NPP 1; NPPase]

ENPP1_HUMAN

Synthetic

Highly Purified

Supplied as a lyophilized powder from acetonitrile/H2O. Reconstitution: Reconstitute with 200ul sterile ddH2O

~0.5 mg/ml (after reconstitution)

Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the orginal vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

ELISA, Antibody blocking - Other applications not tested.

Optimal dilutions to be determined by the researcher.

Testing Data

Molecular Biology; MB-Enzymes, Phosphodiesterase

C-KTHLPTFSQED, from the C Terminus of human ENPP1. Control peptide corresponding to polyclonal antibody, Catalog# MBS623475 , goat x human. Peptide Blocking (see corresponding antibody MBS623475 ): . Antibodies are typically supplied at 0.5mg/ml and peptides as a 100ug pellet. When peptides are reconstituted in 200ul water, the concentration will be 0.5mg/ml. To start, the best ratio would be 1:1 (which means molar excess of peptides relative to antibodies when identical volumes are mixed). Mix equal volumes of peptide and antibody at the required dilution and leave at ambient temperature. It is best is to have two identical blots, to be incubated with equal amount of antibodies, but one with the antibodies pre-adsorbed to the peptide for 20min. Then incubate and develop the two blots in parallel.

170650661

NP_006199.2

NM_006208.2

P22413

Endochondral Ossification Pathway (198812); Insulin Signaling Pathway (198845); Metabolism Pathway (477135); Metabolism Of Vitamins And Cofactors Pathway (106249); Metabolism Of Water-soluble Vitamins And Cofactors Pathway (106250); NAD Salvage Pathway II (545284); Nicotinate And Nicotinamide Metabolism Pathway (83014); Nicotinate And Nicotinamide Metabolism Pathway (400); Pantothenate And CoA Biosynthesis Pathway (83015); Pantothenate And CoA Biosynthesis Pathway (401)

This gene is a member of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. The encoded protein is a type II transmembrane glycoprotein comprising two identical disulfide-bonded subunits. This protein has broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. This protein may function to hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and may also hydrolyze diadenosine polyphosphates. Mutations in this gene have been associated with 'idiopathic' infantile arterial calcification, ossification of the posterior longitudinal ligament of the spine (OPLL), and insulin resistance. [provided by RefSeq, Jul 2008]

Function: By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity. Ref.10. Catalytic activity: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.A dinucleotide + H2O = 2 mononucleotides. Cofactor: Binds 2 divalent metal cations per subunit . By similarity. Enzyme regulation: At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis. Subunit structure: The secreted form is monomeric . By similarity. Homodimer; disulfide-linked. Interacts with INSR. Ref.10. Subcellular location: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted . By similarity. Note: The proteolytically processed form is secreted . By similarity. Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side. Ref.11 Ref.12. Tissue specificity: Expressed in plasma cells and also in a number of non-lymphoid tissues, including the distal convoluted tubule of the kidney, chondrocytes and epididymis. Ref.9. Domain: The di-leucine motif is required for basolateral targeting in epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells . By similarity. Post-translational modification: Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.N-glycosylated.It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.The interchain disulfide bonding resides in the transmembrane segment . By similarity.A secreted form is produced through cleavage at Lys-103 by intracellular processing . By similarity. Involvement in disease: Ossification of the posterior longitudinal ligament of the spine (OPLL) [MIM:602475]: A calcification of the posterior longitudinal ligament of the spinal column, usually at the level of the cervical spine. Patients with OPLL frequently present with a severe myelopathy that can lead to tetraparesis.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16Arterial calcification of infancy, generalized, 1 (GACI1) [MIM:208000]: A severe autosomal recessive disorder characterized by calcification of the internal elastic lamina of muscular arteries and stenosis due to myointimal proliferation. The disorder is often fatal within the first 6 months of life because of myocardial ischemia resulting in refractory heart failure.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.20 Ref.24Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19Hypophosphatemic rickets, autosomal recessive, 2 (ARHR2) [MIM:613312]: A hereditary form of hypophosphatemic rickets, a disorder of proximal renal tubule function that causes phosphate loss, hypophosphatemia and skeletal deformities, including rickets and osteomalacia unresponsive to vitamin D. Symptoms are bone pain, fractures and growth abnormalities.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22. Sequence similarities: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.Contains 2 SMB (somatomedin-B) domains. Caution: It is uncertain whether Met-1 or Met-53 is the initiator. Sequence caution: The sequence AAA63237.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.The sequence AAH59375.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.The sequence BAA02054.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

0.1 mg

400 USD