癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
PEN2 Antibody
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IF, E, IHC-P |
|---|---|
| Primary Accession | Q9NZ42 |
| Other Accession | NP_758844, 28144920 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 12029 Da |
| Concentration (mg/ml) | 1 mg/mL |
| Conjugate | Unconjugated |
| Application Notes | PEN2 antibody can be used for detection of PEN2 by Western blot at 0.5 - 1 µg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 µg/mL. For immunofluorescence start at 20 µg/mL. |
| Gene ID | 55851 |
|---|---|
| Other Names | PEN2 Antibody: PEN2, PEN-2, MDS033, MSTP064, PEN2, Gamma-secretase subunit PEN-2, Presenilin enhancer protein 2, presenilin enhancer 2 homolog (C. elegans) |
| Target/Specificity | PSENEN; |
| Reconstitution & Storage | PEN2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | PEN2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PSENEN |
|---|---|
| Synonyms | PEN2 |
| Function | Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein) (PubMed:12522139, PubMed:12679784, PubMed:12740439, PubMed:12763021, PubMed:24941111, PubMed:30598546, PubMed:30630874). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity (PubMed:12522139, PubMed:12679784, PubMed:12740439, PubMed:12763021, PubMed:24941111). |
| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein Note=Predominantly located in the endoplasmic reticulum and in the cis- Golgi. |
| Tissue Location | Widely expressed. Expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, skeletal muscle, heart and 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
PEN2 Antibody: PEN2, in addition to presenilin, nicastrin, and APH-1 forms the gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease.
REFERENCES
Weihofen A and Martoglio B. Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol. 2003; 13:71-8.
Periz G and Fortini ME. Functional reconstitution of g-secretase through coordinated expression of presenilin, nicastrin, aph-1, and pen-2. J. Neurosci. Res. 2004; 77:309-22.
Selkoe DJ. The cell biology of b-amyloid precursor protein and presenilin in Alzheimer’s disease. Trends Cell Biol. 1998; 8:447-53.
Selkoe SJ. Translating cell biology into therapeutic advances in Alzheimer’s disease. Nature 1999; 399:A23-31
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