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Purified Mouse anti-PKCα (pT497)
Purified Mouse anti-PKCα (pT497)
Western blot analysis of PKCα (pT497) in human T leukemia.  Lysates from Jurkat cell line were probed with purified mouse anti-PKCα (pT497) monoclonal antibody at concentrations of 4.0 (lanes 1 and 4), 2.0 (lanes 2 and 5), and 1.0 µg/ml (lanes 3 and 6) with (lanes 1-3) or without (lanes 4-6) lambda protein phosphatase treatment.  PKCα (pT497) is identified as a band of 75 kDa in the untreated lysate.
Western blot analysis of PKCα (pT497) in human T leukemia.  Lysates from Jurkat cell line were probed with purified mouse anti-PKCα (pT497) monoclonal antibody at concentrations of 4.0 (lanes 1 and 4), 2.0 (lanes 2 and 5), and 1.0 µg/ml (lanes 3 and 6) with (lanes 1-3) or without (lanes 4-6) lambda protein phosphatase treatment.  PKCα (pT497) is identified as a band of 75 kDa in the untreated lysate.
Product Details
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BD Pharmingen™
Mouse BALB/c IgG1, κ
Phosphorylated Human PKCα Peptide
Western blot (Routinely Tested)
75 kDa
0.5 mg/ml
Aqueous buffered solution containing ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at 4°C.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
558379 Rev. 1
Antibody Details
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K14-984

The Protein Kinase C (PKC) family of serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion.  Three categories exist, conventional PKC (cPKC), novel PKC (nPKC), and atypical PKC (aPKC).  All have C-terminal kinase domains, which are closely related to those of protein kinases A and B (Akt), and variable N-terminal regulatory domains that give them different modes of activation.  For example, cPKC (α, βI, βII, and γ isoforms) are calcium-activated, phospholipid-dependent serine/threonine-specific enzymes that can also be activated by phorbol esters.  However, nPKC (δ, ε, η, and θ isoforms) and aPKC (ζ, ι, and λ isoforms) are Ca2+-independent.  aPKC are unique in that their activity is independent of diacylglycerols and phorbol esters.  Phosphorylation at three conserved sites in the kinase domain is required for catalytic activity.  Specifically, the threonine 497 (T497) of PKCα is in the activation loop of the kinase domain and is phosphorylated by the constitutively active phosphoinositide-dependent kinase-1 (PDK-1).

The K14-984 monoclonal antibody recognizes the phosphorylated T497 in the kinase domain of human PKCα.

558379 Rev. 1
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
558379 Rev.1
Citations & References
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Development References (1)

  1. Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J. 2003; 370:361-371. (Biology). View Reference
558379 Rev. 1

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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.