Anti-phospho-Akt (Thr308), clone 50-1C-25

Anti-phospho-Akt (Thr308), clone 50-1C-25

05-802

Upstate (Millipore)

Detects Akt only when phosphorylated on Thr308.

60 kDa

KLH-conjugated synthetic peptide containing the Thr308 sequence and surrounding amino acids of human, mouse, rat, bovine and chicken Akt1.

Phosphorylation

NL50

IgG

Akt/PKB is a Ser/Thr kinase and a major known effecter of the PI3 Kinase pathway. It is involved in multiple signaling pathways that relate to many biological processes including metabolism, apoptosis, cell cycle control, angiogenesis, differentiation, and cell growth and proliferation. In mammals, three isoforms of Akt (Akt1/PKCα, Akt2/PKBβ, and Akt3/PKBγ) exists. They exhibit a high degree of homology, but differ slightly in the localization of their regulatory phosphorylation sites. Akt1 is the predominant isoform that is in most tissues and is thought to have a dominant role in growth, survival, embryonic development, and adipocyte differentiation. Akt2 is correlated with the regulation of glucose homeostasis and is the predominant isoform expressed in insulin-responsive tissues. Akt3 is abundant in brain tissue. Each Akt isoform is composed of three functionally distinct regions: an N-terminal Pleckstrin Homology (PH) domain that provides a lipid-binding module, a central catalytic domain containing Thr308, and a C-terminal hydrophobic motif containing Ser473. The activation of AKT is dependent on a dual regulatory mechanism that requires both its translocation to the plasma membrane and dual phosphorylation on Thr308 and Ser473 by PDK1 and the TORC2 complex, respectively.

• Human
• Mouse
• Rabbit
• Bovine
• Chicken

Human and Mouse

Western Blot Analysis:
This lot detected Akt when phosphorylated on Thr308 at 1:1,000 dilution in PDGF-treated NIH/3T3 lysates via SDS-PAGE and transferred to PVDF (Immobilon-P).

This lot detected Akt when phosphorylated on Thr308 at 1:1,000 dilution in PDGF-treated NIH/3T3 lysates via SDS-PAGE and transferred to PVDF (Immobilon-P).

Protein A purfied

Protein A purified recombinant rabbit monoclonal supernatant in 0.1M Tris-Glycine (pH7.4) 150mM NaCl, and 0.05% NaN3 with 40% glycerol.

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

P31749

NP_001014431

• AKT
• C-AKT
• EC 2.7.11.1
• MGC99656
• PKB
• PKB-ALPHA
• PRKBA
• RAC
• RAC-ALPHA
• RAC-PK-alpha

• Protein kinase B
• RAC-alpha serine/threonine-protein kinase
• murine thymoma viral (v-akt) oncogene homolog-1
• rac protein kinase alpha
• v-akt murine thymoma viral oncogene homolog 1

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

• Western Blotting
• Immunofluorescence
• Immunocytochemistry
• ELISA

The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq]

FUNCTION: SwissProt: P31749 # 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.
SIZE: 480 amino acids; 55686 Da
SUBUNIT: Interacts with CENTG1 isoform 2 (PIKE-A) in the presence of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN. Interacts with AKTIP.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1).
TISSUE SPECIFICITY: In all human cell types so far analyzed.
DOMAIN: SwissProt: P31749 Binding of the PH domain to the phosphatidylinositol 3- kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by the Rictor-mTor complex favors Thr-308 phosphorylation by PDPK1. Ser-473 phosphorylation is enhanced by interaction with CENTG1 isoform 2 (PIKE-A).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. & Contains 1 AGC-kinase C-terminal domain. & Contains 1 PH domain. & Contains 1 protein kinase domain.

Upstate

Akt is the major known effector of the PI3 Kinase pathway. Generation of PIP3 results in the activation of PDK1, which phosphorylates Akt on Thr308, and another kinase complex, thought to be the mTORC2 complex (or possibly an intermediate kinase linking the two) that phosphorylates Akt on Ser473. These phosphorylations additively activate Akt Ser/Thr kinase activity, and the use of phosphorylation state-specific antibodies directed against either of these sites can imply Akt activation. Activation of Akt can be measured directly by immunoprecipitation followed by phosphorylation of a known substrate with radiolabeled ATP. Akt has been shown to phosphorylate over 70 substrates including TSC1&2 in the mTOR pathway, Bad on Ser136, GSK3, which is inactivated by this phosphorylation, the FoxO family of transcription factors, PRAS40, AS160.

Anti-phospho-Akt (Thr308), clone 50-1C-25

Monoclonal Antibody

100 μL

Purified

Rabbit