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Anti-eNOS (C-terminal region) Antibody

     
  • 1 - Anti-eNOS (C-terminal region) Antibody AN1863
    Western blot analysis of human umbilical vein endothelial cells treated with calyculin A (100 nM) for 30 min. (lanes 1, 3, 5 & 7) then the blots were treated with lambda phosphatase (lanes 2, 4, 6 & 8). The blots were probed with anti-endothelial nitric oxide synthase (eNOS) (C-terminal region) (lanes 1 & 2), anti-eNOS (Ser-632) (lanes 3 & 4), anti-eNOS (Ser-1177) (lanes 5 & 6) and anti-eNOS (a.a. 1172-1181) (lanes 7 & 8).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P29474
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 133275 Da
Additional Information
Gene ID 4846
Other Names endothelial Nitric Oxide Synthase, eNOS, ecNOS, NOS-III, NOS3, NOSIII
Dilution WB~~1:1000
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-eNOS (C-terminal region) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH, and oxygen) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin, and heme). Several distinct NOS isoforms are produced from three distinct genes. The inducible form of NOS, iNOS (NOS-II), is Ca2+ independent and is expressed in a broad range of cell types, and two constitutive Ca2+/CaM-dependent forms of NOS: nNOS (bNOS, NOS-I) identified in neurons and eNOS (ecNOS, NOS-III) identified in endothelial cells. Regulation of eNOS activity occurs through phosphorylation at multiple sites. Phosphorylation of Ser-633 (mouse Ser-632) in the FMN binding domain increases eNOS activity and may be important for the maintenance of NO synthesis after initial activation by Ca2+ flux and Ser-1177 phosphorylation.

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