Phospho-NCF1/p47-phox (Ser304) Antibody - #AF7227
(1)
(5)
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# AF7227, RRID:AB_2843667.
展开/折叠
47 kDa autosomal chronic granulomatous disease protein; 47 kDa neutrophil oxidase factor; NADPH oxidase organizer 2; NCF 47K; NCF-1; NCF-47K; Ncf1; NCF1_HUMAN; Neutrophil cytosol factor 1; Neutrophil cytosolic factor 1; neutrophil cytosolic factor 1, (chronic granulomatous disease, autosomal 1); Neutrophil NADPH oxidase factor 1; Nox organizer 2; Nox organizing protein 2; Nox-organizing protein 2; NOXO2; p47 phox; p47-phox; SH3 and PX domain containing protein 1A; SH3 and PX domain-containing protein 1A; SH3PXD1A;
抗原和靶标
- P14598 NCF1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV
种属预测
score>80的预测可信度较高，可尝试用于WB检测。*预测模型主要基于免疫原序列比对，结果仅作参考，不作为质保凭据。
High(score>80) Medium(80>score>50) Low(score<50) No confidence
翻译修饰 - P14598 作为底物
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| Y41 | Phosphorylation | Uniprot | |
| T45 | Phosphorylation | Uniprot | |
| Y48 | Phosphorylation | Uniprot | |
| T133 | Phosphorylation | Q9NWZ3 (IRAK4) | Uniprot |
| T138 | Phosphorylation | Q9NWZ3 (IRAK4) | Uniprot |
| Y139 | Phosphorylation | Uniprot | |
| T153 | Phosphorylation | Q9NWZ3 (IRAK4) | Uniprot |
| S208 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
| Y279 | Phosphorylation | Uniprot | |
| S283 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
| S288 | Phosphorylation | Q9NWZ3 (IRAK4) | Uniprot |
| S303 | Phosphorylation | P17252 (PRKCA) , Q05513 (PRKCZ) , Q05655 (PRKCD) , P05771 (PRKCB) | Uniprot |
| S304 | Phosphorylation | Q05513 (PRKCZ) , P05771-2 (PRKCB) , P17252 (PRKCA) , P31749 (AKT1) , Q05655 (PRKCD) | Uniprot |
| S310 | Phosphorylation | Uniprot | |
| S315 | Phosphorylation | P05771 (PRKCB) , P17252 (PRKCA) , Q05513 (PRKCZ) , Q05655 (PRKCD) | Uniprot |
| S320 | Phosphorylation | Q9NWZ3 (IRAK4) , P17612 (PRKACA) , P05771-2 (PRKCB) , Q05513 (PRKCZ) , Q05655 (PRKCD) , P17252 (PRKCA) | Uniprot |
| S328 | Phosphorylation | Q05655 (PRKCD) , P31749 (AKT1) , P17252 (PRKCA) , P17612 (PRKACA) , Q05513 (PRKCZ) , P05771 (PRKCB) | Uniprot |
| S345 | Phosphorylation | Q16539 (MAPK14) , Q9NWZ3 (IRAK4) , P28482 (MAPK1) , P27361 (MAPK3) | Uniprot |
| S348 | Phosphorylation | P68400 (CSNK2A1) , P28482 (MAPK1) , P27361 (MAPK3) , Q9NWZ3 (IRAK4) , Q16539 (MAPK14) | Uniprot |
| T356 | Phosphorylation | Q9NWZ3 (IRAK4) | Uniprot |
| S359 | Phosphorylation | Q9NWZ3 (IRAK4) , Q05513 (PRKCZ) , P05771-2 (PRKCB) , P17252 (PRKCA) , Q05655 (PRKCD) , P17612 (PRKACA) | Uniprot |
| S370 | Phosphorylation | Q05513 (PRKCZ) , Q9NWZ3 (IRAK4) , P05771 (PRKCB) , Q05655 (PRKCD) , P17612 (PRKACA) , P17252 (PRKCA) | Uniprot |
| S379 | Phosphorylation | Q05513 (PRKCZ) , Q05655 (PRKCD) , P05771 (PRKCB) , P17252 (PRKCA) | Uniprot |
| S381 | Phosphorylation | Uniprot | |
| T382 | Phosphorylation | Uniprot |
研究背景
NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity.
Cytoplasm>Cytosol. Membrane>Peripheral membrane protein>Cytoplasmic side.
Detected in peripheral blood monocytes and neutrophils (at protein level).
Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG. Interacts with PARK7 (via C-terminus); the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (By similarity).
The PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state.
研究领域
· Cellular Processes > Transport and catabolism > Phagosome. (View pathway)
· Human Diseases > Infectious diseases: Parasitic > Leishmaniasis.
· Organismal Systems > Immune system > Chemokine signaling pathway. (View pathway)
· Organismal Systems > Development > Osteoclast differentiation. (View pathway)
· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis. (View pathway)
· Organismal Systems > Immune system > Leukocyte transendothelial migration. (View pathway)
文献引用
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