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>   首页   >   Anti-NF-kB p65 (Ser316) Antibody   

Anti-NF-kB p65 (Ser316) Antibody

Our Anti-NF-kB p65 (Ser316) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions

     
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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 Q04207
Host Rabbit
Clonality Polyclonal
Isotype IgG
Calculated MW 60212 Da
Additional Information
Gene ID 19697
Other Names Avian reticuloendotheliosis viral (v rel) oncogene homolog A antibody, MGC131774 antibody, NF kappa B p65delta3 antibody, NFKB3 antibody, Nuclear Factor NF Kappa B p65 Subunit antibody, Nuclear factor NF-kappa-B p65 subunit antibody, Nuclear factor of kappa light polypeptide gene enhancer in B cells 3 antibody, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3 antibody, OTTHUMP00000233473 antibody, OTTHUMP00000233474 antibody, OTTHUMP00000233475 antibody, OTTHUMP00000233476 antibody, OTTHUMP00000233900 antibody, p65 antibody, p65 NF kappaB antibody, p65 NFkB antibody, relA antibody, TF65_HUMAN antibody, Transcription factor p65 antibody, v rel avian reticuloendotheliosis viral oncogene homolog A (nuclear factor of kappa light polypeptide gene enhancer in B cells 3 (p65)) antibody, V rel avian reticuloendotheliosis viral oncogene homolog A antibody, v rel reticuloendotheliosis viral oncogene homolog A (avian) antibody, V rel reticuloendotheliosis viral oncogene homolog A nuclear factor of kappa light polypeptide gene enhancer in B cells 3 p65 antibody
Target/Specificity p65, also known as RelA, is one of the five members of the NF-kB family. The p65 and p50 heterodimer is the predominant form of NF-kB, where p65 is the major subunit (Gilmore et al, 2006). There have been 13 identified phosphorylation sites on p65, including Ser-316 which is induced by IL-1β (Viatour et al, 2005 and Wang et al, 2015). Phosphorylation of Ser-316 is essential for NF-kB nuclear transportation, NF-kB-dependent gene regulation, cytokine/chemokine secretion, and other biological functions (Wang et al, 2015). Ser-316 has also been demonstrated to co-phosphorylate with either Ser-529 or Ser-536 to regulate the majority of NF-kB targeted genes while having its own unique regulation function (Wang et al, 2015). CKI kinase specifically targets phosphorylation at Ser-316 on p65 (Wang et al, 2015). CKI is involved in regulation of membrane transport, cell division, DNA repair, and nuclear localization by phosphorylating its target proteins (Price et al, 2006).
Dilution WB~~1:1000
Format Antigen Affinity Purified from Pooled Serum
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-NF-kB p65 (Ser316) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice

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

BACKGROUND

p65, also known as RelA, is one of the five members of the NF-kB family. The p65 and p50 heterodimer is the predominant form of NF-kB, where p65 is the major subunit (Gilmore et al, 2006). There have been 13 identified phosphorylation sites on p65, including Ser-316 which is induced by IL-1β (Viatour et al, 2005 and Wang et al, 2015). Phosphorylation of Ser-316 is essential for NF-kB nuclear transportation, NF-kB-dependent gene regulation, cytokine/chemokine secretion, and other biological functions (Wang et al, 2015). Ser-316 has also been demonstrated to co-phosphorylate with either Ser-529 or Ser-536 to regulate the majority of NF-kB targeted genes while having its own unique regulation function (Wang et al, 2015). CKI kinase specifically targets phosphorylation at Ser-316 on p65 (Wang et al, 2015). CKI is involved in regulation of membrane transport, cell division, DNA repair, and nuclear localization by phosphorylating its target proteins (Price et al, 2006).

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