Cell Signaling Technology

Product Pathways - Lymphocyte Signaling

PKCθ (E1I7Y) Rabbit mAb (PE Conjugate) #86495

No. Size Price
86495S 100 µl ( 50 tests ) ¥3,986.00 现货查询 购买询价
86495 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
F 1:50 Human,Mouse,Rat, Endogenous Rabbit IgG

Species cross-reactivity is determined by western blot.

Applications Key: F=Flow Cytometry,

Homology

Species predicted to react based on 100% sequence homology: Bovine,

Specificity / Sensitivity

PKCθ (E1I7Y) Rabbit mAb (PE Conjugate) recognizes endogenous levels of total PKCθ protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro632 of human PKCθ protein.

Description

This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PKCθ (E1I7Y) Rabbit mAb #13643.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of mouse splenocytes using Rabbit (DA1E) mAb IgG XP® Isotype Control (PE Conjugate) #5742 (left) and PKCθ (E1I7Y) Rabbit mAb (PE Conjugate) (right). Splenocytes were co-stained with anti-CD3 conjugated to APC.

Background

Activation of protein kinase C (PKC) is one of the earliest events in a cascade that 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).

  1. Nishizuka, Y. (1984) Nature 308, 693-8.
  2. Keranen, L.M. et al. (1995) Curr Biol 5, 1394-403.
  3. Mellor, H. and Parker, P.J. (1998) Biochem J 332 ( Pt 2), 281-92.
  4. Ron, D. and Kazanietz, M.G. (1999) FASEB J 13, 1658-76.
  5. Moscat, J. and Diaz-Meco, M.T. (2000) EMBO Rep 1, 399-403.
  6. Baron, C.L. and Malhotra, V. (2002) Science 295, 325-8.
  7. Flynn, P. et al. (2000) J Biol Chem 275, 11064-70.

Application References

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

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

XP is a registered trademark of Cell Signaling Technology, Inc.

Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.

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