Protein Kinase B (PKB) (C-Term) Antikörper

Antigen: Protein Kinase B (PKB)

Synonyme: Akt, PKB, Rac, PKB/Akt, PKBalpha, AKT, RAC, PRKBA, MGC99656, PKB-ALPHA, RAC-ALPHA, PTK, CAKB, FAK2, FRNK, PYK2, CADTK, FADK2, RAFTK

Epitope: C-Term

Klonalität: Polyklonal

Wirt: Kaninchen

Applikation: Immunhistochemie (IHC), Western Blot (WB)

Produktnummer: ABIN350718

Produktbeschreibung

Weitere Bezeichnung: pan AKT (RAC-alpha serine/threonine-protein kinase, PKB, RAC) (c-terminal)

Swiss-Prot: P31750

Immunogen: A synthetic peptide from the c-terminal of mouse AKT1 (RAC-alpha serine/threonine-protein kinase, PKB, RAC) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in rat, human and chicken.

Format: Lyophilized

Beschreibung: FUNCTION: General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ENZYME REGULATION: Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note: Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. TISSUE SPECIFICITY: Widely expressed. Low levels found in liver with slightly higher levels present in thymus and testis. Also known as: RAC-alpha serine/threonine-protein kinase, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, PKB, RAC, AKT1.

Spezifität: Appears to be specific for AKT1, AKT2, AKT3.

Anwendungen

Applikationshinweise: IHC, WB. A dilution of 1 : 300 to 1 : 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.

Reinheit: whole serum

Lagerung: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

WB on rat brain lysate using Rabbit antibody to c-terminal of AKT (RAC-alpha serine/threonine-protein kinase, PKB, RAC): whole serum (ABIN350718) at 1 : 1000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the detected band.

Publikationen

Publikationen: Cong, Chen, Li et al.: "Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells." in: Molecular endocrinology (Baltimore, Md.), Vol. 11, Issue 13, pp. 1881-90, 1998 (PubMed).

Pekarsky, Koval, Hallas et al.: "Tcl1 enhances Akt kinase activity and mediates its nuclear translocation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 7, pp. 3028-33, 2000 (PubMed).

Maira, Galetic, Brazil et al.: "Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane." in: Science (New York, N.Y.), Vol. 294, Issue 5541, pp. 374-80, 2001 (PubMed).

Anai, Shojima, Katagiri et al.: "A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase activity and regulates DNA synthesis." in: The Journal of biological chemistry, Vol. 280, Issue 18, pp. 18525-35, 2005 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).