ENPP1 Rabbit pAb
- 产品详情
- 实验流程
Application
| IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | P06802 |
| Other Accession | P06802 |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 103176 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from mouse ENPP1 |
| Epitope Specificity | 851-900/925 |
| Isotype | IgG |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SIMILARITY | Belongs to the peptidase S8 family. Furin subfamily. |
| SUBUNIT | Homodimer; disulfide-linked. |
| Post-translational modifications | 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. |
| DISEASE | Defects in PCSK1 are the cause of proprotein convertase 1 deficiency (PC1 deficiency) [MIM:600955]. PC1 deficiency is characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small-intestinal absorptive dysfunction It is due to impaired processing of prohormones. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | ENPP1 has a broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. It can hydrolyze nucleoside 5' triphosphates such as ATP, GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate. It can also hydrolyze diadenosine polyphosphates and 3',5'-cAMP to AMP. It may play a role in the regulation of pyrophosphate production, the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. The subtilisin-like Prohormone Convertase (PC) family is a group of cellular enzymes that cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. PC family members share structural similarities, which include a heterogeneous ~10 kDa amino-terminal proregion, a highly conserved ~55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. The subcellular localization of PC family members varies. Immunolocalization studies show that PC1 is found in the perinuclear region as well as the trans-Golgi network, whereas PC2 can be found in the trans-Golgi network as well as diffusely distributed in the peripheral cytoplasm. |
| Gene ID | 18605 |
|---|---|
| Other Names | ARHR2; COLED; M6S1; NPP1; NPPS; PC-1; PCA1; PDNP1; 4833416E15Rik; CD203c; E-NPP 1; E-NPP1; Ly-41; Pca; Pca-1; ttw; twy; Pc1; ENPP1_HUMAN; ENPP1; Alkaline phosphodiesterase I; Membrane component chromosome 6 surface marker 1; Nucleotide diphosphatase; Nucleotide pyrophosphatase (NPPase); Phosphodiesterase I/nucleotide pyrophosphatase 1; Plasma-cell membrane glycoprotein PC-1; ENPP1_MOUSE; Lymphocyte antigen 41 (Ly-41); ENPP1_RAT; ectonucleotide pyrophosphatase/phosphodiesterase 1 |
| Dilution | IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500 |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | Enpp1 {ECO:0000303|PubMed:23027977, ECO:0000312|MGI:MGI:97370} |
|---|---|
| Function | Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930, PubMed:9662402). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:19419305, PubMed:22510396, PubMed:25260930, PubMed:25479107, PubMed:26910915, PubMed:30111653, PubMed:35147247, PubMed:9662402). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:11027689, PubMed:1647027, PubMed:23027977, PubMed:8223581). 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 (PubMed:1647027). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (PubMed:30111653). Appears to modulate insulin sensitivity (By similarity). Also involved in melanogenesis (By similarity). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (By similarity). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3',3'-cGAMP (By similarity). |
| Cellular Location | [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1]: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. |
| Tissue Location | Selectively expressed on the surface of antibody- secreting cells (PubMed:3104326). Expressed in osteocytes and osteoclasts (PubMed:25260930). |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
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