NSMase2 Rabbit pAb
NSMase2 Rabbit pAb
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Application
| IHC-P, IHC-F, IF, E |
|---|---|
| Primary Accession | Q9NY59 |
| Reactivity | Human, Mouse, Rat |
| Predicted | Dog, Pig, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 71081 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human NSMase2 |
| Epitope Specificity | 511-610/655 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Golgi apparatus membrane. Cell membrane. May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons. According to PubMed:15051724, it localizes to plasma membrane in confluent contact-inhibited cells. |
| SIMILARITY | Belongs to the neutral sphingomyelinase family. |
| SUBUNIT | Belongs to the neutral sphingomyelinase family. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | N-SMase2 (neutral sphingomyelinase 2), also known as NSMASE2 or SMPD3 (sphingomyelin phosphodiesterase 3), is a ubiquitously expressed 655 amino acid member of the magnesium-dependent phosphohydrolase protein family. Localized to the membrane of the Golgi apparatus, N-SMase2 functions to catalyze the hydrolysis of sphingomyelin to form ceramide and phosphocholine—two proteins that mediate cell growth arrest and apoptosis. N-SMase2 is enzymatically activated by unsaturated fatty acids and phosphatidylserine and, through regulation of ceramide synthesis, is involved in growth suppression and postnatal development. Expression of N-SMase2 is upregulated during the G0/G1 phases of the cell cycle and optimal N-SMase2 activity occurs at a slightly basic pH of 7.5. N-SMase2 deficiency is the cause of chondrodysplasia, a genetic disorder characterized by impaired bone growth that leads to short stature, bowlegs and underdeveloped joints. |
| Gene ID | 55512 |
|---|---|
| Other Names | Sphingomyelin phosphodiesterase 3, 3.1.4.12, Neutral sphingomyelinase 2, nSMase-2, nSMase2, Neutral sphingomyelinase II, SMPD3 (HGNC:14240) |
| Target/Specificity | Predominantly expressed in brain. |
| Dilution | IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ELISA=1:5000-10000 |
| 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. |
| Name | SMPD3 (HGNC:14240) |
|---|---|
| Function | Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). |
| Cellular Location | Golgi apparatus membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:10823942). Localizes to plasma membrane in confluent contact- inhaibited cells (PubMed:15051724) |
| Tissue Location | Predominantly expressed in brain. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
N-SMase2 (neutral sphingomyelinase 2), also known as NSMASE2 or SMPD3 (sphingomyelin phosphodiesterase 3), is a ubiquitously expressed 655 amino acid member of the magnesium-dependent phosphohydrolase protein family. Localized to the membrane of the Golgi apparatus, N-SMase2 functions to catalyze the hydrolysis of sphingomyelin to form ceramide and phosphocholine—two proteins that mediate cell growth arrest and apoptosis. N-SMase2 is enzymatically activated by unsaturated fatty acids and phosphatidylserine and, through regulation of ceramide synthesis, is involved in growth suppression and postnatal development. Expression of N-SMase2 is upregulated during the G0/G1 phases of the cell cycle and optimal N-SMase2 activity occurs at a slightly basic pH of 7.5. N-SMase2 deficiency is the cause of chondrodysplasia, a genetic disorder characterized by impaired bone growth that leads to short stature, bowlegs and underdeveloped joints.
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