AKT1 Human

Protein Kinase B Alpha Human Recombinant
Cat. No.
BT8592
Source
Escherichia Coli.
Synonyms
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

AKT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-480 a.a) and having a molecular mass of 58.1kDa.
AKT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Akt1, also called Akt or protein kinase B (PKB), is a crucial molecule for cellular signaling in mammals. Humans possess three genes within the "Akt family": Akt1, Akt2, and Akt3. These enzymes belong to the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 plays a vital role in cell survival pathways by suppressing apoptotic processes. It can also stimulate protein synthesis pathways, making it a key signaling protein for cellular pathways that lead to skeletal muscle hypertrophy and overall tissue growth. Due to its ability to inhibit apoptosis and promote cell survival, Akt1 is implicated as a significant factor in various cancers. Initially, Akt (now referred to as Akt1) was identified as the oncogene in the AKT8 transforming retrovirus.
Description
Recombinant human AKT1, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-480 a.a) with a molecular mass of 58.1 kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
AKT1 protein solution (0.5 mg/ml) in 20 mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), store the entire vial at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity exceeds 85% as determined by SDS-PAGE analysis.
Synonyms
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSDVAIV KEGWLHKRGE YIKTWRPRYF LLKNDGTFIG YKERPQDVDQ REAPLNNFSV AQCQLMKTER PRPNTFIIRC LQWTTVIERT FHVETPEERE EWTTAIQTVA DGLKKQEEEE MDFRSGSPSD NSGAEEMEVS LAKPKHRVTM NEFEYLKLLG KGTFGKVILV KEKATGRYYA MKILKKEVIV AKDEVAHTLT ENRVLQNSRH PFLTALKYSF QTHDRLCFVM EYANGGELFF HLSRERVFSE DRARFYGAEI VSALDYLHSE KNVVYRDLKL ENLMLDKDGH IKITDFGLCK EGIKDGATMK TFCGTPEYLA PEVLEDNDYG RAVDWWGLGV VMYEMMCGRL PFYNQDHEKL FELILMEEIR FPRTLGPEAK SLLSGLLKKD PKQRLGGGSE DAKEIMQHRF FAGIVWQHVY EKKLSPPFKP QVTSETDTRY FDEEFTAQMI TITPPDQDDS MECVDSERRP HFPQFSYSAS GTA.

Product Science Overview

Structure and Activation

PKBα is composed of three main domains:

  1. Pleckstrin Homology (PH) Domain: This domain is responsible for binding phosphoinositides, which helps in the recruitment of PKBα to the plasma membrane.
  2. Kinase Domain: This domain is responsible for the enzyme’s catalytic activity.
  3. Regulatory Domain: This domain contains sites for phosphorylation, which are crucial for the activation of PKBα .

In its inactive state, PKBα resides in the cytosol. Upon cellular stimulation, such as through insulin or growth factors, phosphoinositide 3-kinase (PI3K) generates lipid products that recruit PKBα to the plasma membrane. Here, PKBα undergoes phosphorylation at two key residues: Thr308 in the kinase domain and Ser473 in the regulatory domain. This phosphorylation fully activates PKBα, enabling it to phosphorylate downstream targets .

Functions and Significance

PKBα is a major mediator of the cellular responses to insulin and insulin-like growth factor 1 (IGF1). It plays a pivotal role in:

  • Glucose Metabolism: PKBα facilitates glucose uptake by promoting the translocation of glucose transporter 4 (GLUT4) to the cell membrane.
  • Cell Survival: PKBα inhibits apoptosis by phosphorylating and inactivating components of the apoptotic machinery, such as BAD and caspase-9.
  • Cell Growth and Proliferation: PKBα promotes protein synthesis and cell growth by activating the mTOR pathway .
Role in Disease

PKBα is implicated in various diseases, particularly cancer. Its role in promoting cell survival and growth makes it a key player in tumorigenesis. Overactivation of PKBα is often observed in cancers, where it contributes to uncontrolled cell proliferation and resistance to apoptosis . Additionally, PKBα has been linked to metabolic disorders such as diabetes, due to its critical role in insulin signaling .

Recombinant PKBα

Recombinant human PKBα is produced using various expression systems, including baculovirus-insect cells. The recombinant protein is typically purified and formulated for use in research and therapeutic applications. It is used to study the biochemical properties of PKBα, screen for potential inhibitors, and understand its role in various signaling pathways .

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