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Phospho-Akt (Thr308) Polyclonal Antibody, HRP Conjugated

Product Specifications

Background

AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH) domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin) . PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.

Synonyms

AktThr308; C AKT; MGC9965; Oncogene AKT1; PKB; PRKBA; Protein Kinase B Alpha; RAC Alpha; RAC; RAC PK Alpha; RAC Serine/Threonine Protein Kinase; vAKT Murine Thymoma Viral Oncogene Homolog 1; AKT1_HUMAN.

Gene ID

207

Modification Site

Thr308

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat, Bovine

Target

Phospho-Akt (Thr308)

Clonality

Polyclonal

Isotype

IgG

Conjugation

HRP

Source

KLH conjugated synthetic phosphopeptide derived from human Akt around the phosphorylation site of Thr308

Applications

WB, IHC-P, IHC-F

Purification

Purified by Protein A.

Concentration

1µg/µl

Dilution

WB (1:300-5000), IHC-P (1:200-400), IHC-F (1:100-500)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Phosphorylation

Storage Conditions

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Gene ID URL

207

Curated Selection

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