PRKCE-Polyclonal Antibodies

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PRKCE

Qty


Total
$220
Catalog #
A2110
Antibody Type
Polyclonal Antibody
Gene ID
5581
Swiss Prot
Q02156
Size
Species
Rabbit
Isotype
IgG
Purity
Affinity purification
Additional Information
ReactivityHuman Mouse Rat
Tested applicationsWB IHC ICC
Recommended DilutionWB 1:500 - 1:2000 IHC 1:50 - 1:200 ICC 1:50 - 1:200
Calculated MW84kDa
Observed MWRefer to Figures
ImmunogenRecombinant protein of human PRKCE
Storage BufferStore at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentrationbqr
SynonymMGC125656; MGC125657; PKCE; nPKC-epsilon;
Images
  • A2110: image 1

    Western blot analysis of extracts of various cell lines, using PRKCE antibody.

  • A2110: image 2

    Immunohistochemistry of paraffin-embedded rat spleen using PRKCE antibody at dilution of 1:200 (x400 lens).

  • A2110: image 3

    Immunohistochemistry of paraffin-embedded human colon using PRKCE antibody at dilution of 1:200 (x400 lens).

  • A2110: image 4

    Immunohistochemistry of paraffin-embedded human esophageal cancer using PRKCE antibody at dilution of 1:200 (x400 lens).

  • A2110: image 5

    Immunohistochemistry of paraffin-embedded Human gastric using PRKCE antibody at dilution of 1:100 (x400 lens).

  • A2110: image 6

    Immunohistochemistry of paraffin-embedded Human kidney using PRKCE antibody at dilution of 1:100 (x400 lens).

Background

at controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

Protocol

N/A

MSDS
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