Recombinant Human Akt1 Protein, His and Strep-tagged
Cat.No. : | Akt1-810H |
Product Overview : | Recombinant human Akt1 protein with His and Strep tag was expressed in HEK293. |
- Specification
- Gene Information
- Related Products
- Download
Description : | This gene encodes one of the three members of the human AKT serine-threonine protein kinase family which are often referred to as protein kinase B alpha, beta, and gamma. These highly similar AKT proteins all have an N-terminal pleckstrin homology domain, a serine/threonine-specific kinase domain and a C-terminal regulatory domain. These proteins are phosphorylated by phosphoinositide 3-kinase (PI3K). AKT/PI3K forms a key component of many signalling pathways that involve the binding of membrane-bound ligands such as receptor tyrosine kinases, G-protein coupled receptors, and integrin-linked kinase. These AKT proteins therefore regulate a wide variety of cellular functions including cell proliferation, survival, metabolism, and angiogenesis in both normal and malignant cells. AKT proteins are recruited to the cell membrane by phosphatidylinositol 3,4,5-trisphosphate (PIP3) after phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) by PI3K. Subsequent phosphorylation of both threonine residue 308 and serine residue 473 is required for full activation of the AKT1 protein encoded by this gene. Phosphorylation of additional residues also occurs, for example, in response to insulin growth factor-1 and epidermal growth factor. Protein phosphatases act as negative regulators of AKT proteins by dephosphorylating AKT or PIP3. The PI3K/AKT signalling pathway is crucial for tumor cell survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating AKT1 which then phosphorylates and inactivates components of the apoptotic machinery. AKT proteins also participate in the mammalian target of rapamycin (mTOR) signalling pathway which controls the assembly of the eukaryotic translation initiation factor 4F (eIF4E) complex and this pathway, in addition to responding to extracellular signals from growth factors and cytokines, is disregulated in many cancers. Mutations in this gene are associated with multiple types of cancer and excessive tissue growth including Proteus syndrome and Cowden syndrome 6, and breast, colorectal, and ovarian cancers. Multiple alternatively spliced transcript variants have been found for this gene. |
Source : | HEK293 |
Species : | Human |
Tag : | His&Strep |
Form : | Lyophilized |
Molecular Mass : | 59.5 kDa |
Protein length : | 480 |
AA Sequence : | MSDVAIVKEGWLHKRGEYIKTWRPR YFLLKNDGTFIGYKERPQDVDQREA PLNNFSVAQCQLMKTERPRPNTFII RCLQWTTVIERTFHVETPEEREEWT TAIQTVADGLKKQEEEEMDFRSGSP SDNSGAEEMEVSLAKPKHRVTMNEF EYLKLLGKGTFGKVILVKEKATGRY YAMKILKKEVIVAKDEVAHTLTENR VLQNSRHPFLTALKYSFQTHDRLCF VMEYANGGELFFHLSRERVFSEDRA RFYGAEIVSALDYLHSEKNVVYRDL KLENLMLDKDGHIKITDFGLCKEGI KDGATMKTFCGTPEYLAPEVLEDND YGRAVDWWGLGVVMYEMMCGRLPFY NQDHEKLFELILMEEIRFPRTLGPE AKSLLSGLLKKDPKQRLGGGSEDAK EIMQHRFFAGIVWQHVYEKKLSPPF KPQVTSETDTRYFDEEFTAQMITIT PPDQDDSMECVDSERRPHFPQFSYS ASGTA |
Purity : | > 98% |
Applications : | WB; ELISA; FACS; FC |
Stability : | This bioreagent is stable at 4 centigrade (short-term) and -70 centigrade(long-term). After reconstitution, sample may be stored at 4 centigrade for 2-7 days and below -18 centigrade for future use. |
Storage : | At -20 centigrade. |
Concentration : | 1 mg/mL |
Storage Buffer : | PBS (pH 7.4-7.5). Sterile-filtered colorless solution. |
Reconstitution : | Reconstitute in sterile distilled H2O to no less than 100 μg/mL; dilute reconstituted stock further in other aqueous solutions if needed. Please review COA for lot-specific instructions. Final measurements should be determined by the end-user for optimal performance. |
Gene Name : | AKT1 v-akt murine thymoma viral oncogene homolog 1 [ Homo sapiens (human) ] |
Official Symbol : | Akt1 |
Synonyms : | AKT1; v-akt murine thymoma viral oncogene homolog 1; RAC-alpha serine/threonine-protein kinase; AKT; PKB; PRKBA; RAC; PKB alpha; RAC-PK-alpha; proto-oncogene c-Akt; protein kinase B alpha; rac protein kinase alpha; PKB-ALPHA; RAC-ALPHA; MGC99656; |
Gene ID : | 207 |
mRNA Refseq : | NM_001014431 |
Protein Refseq : | NP_001014431 |
MIM : | 164730 |
UniProt ID : | P31749 |
Products Types
◆ Recombinant Protein | ||
Akt1-566M | Recombinant Mouse Akt1 Protein, MYC/DDK-tagged | +Inquiry |
AKT1-0080H | Recombinant Human AKT1 Protein (M1-A480), Tag Free | +Inquiry |
AKT1-0081H | Recombinant Human AKT1 Protein (M1-A480), GST tagged | +Inquiry |
AKT1-014H | Recombinant Human AKT1 Protein, MYC/DDK-tagged, C13 and N15-labeled | +Inquiry |
AKT1-306H | Recombinant Human AKT1 Protein, His (Fc)-Avi-tagged | +Inquiry |
◆ Lysates | ||
AKT1-677HCL | Recombinant Human AKT1 cell lysate | +Inquiry |
Related Gene
Not For Human Consumption!
Inquiry
- Reviews
- Q&As
Customer Reviews (1)
Write a reviewThe manufacturer's dedicated and knowledgeable support team is readily available to address any concerns, provide guidance, and offer timely solutions.
Q&As (13)
Ask a questionYes, several drugs and agents have been developed to specifically target AKT1. These include small molecule inhibitors that directly target the kinase activity of AKT1. Examples of AKT1 inhibitors currently under investigation or in clinical trials include MK-2206, ipatasertib, and capivasertib. These inhibitors aim to block the activation of AKT1 and disrupt its downstream signaling pathways.
Yes, there are inhibitors that specifically target the activity of AKT1 protein. Small molecule inhibitors, such as MK-2206 and GSK690693, have been developed to block AKT1 activation and downstream signaling. These inhibitors are being studied as potential therapeutic agents for cancer treatment. Additionally, certain natural compounds, including resveratrol and curcumin, have been reported to inhibit AKT1 activity and exhibit anti-tumor effects.
Mutations in AKT1 have been implicated in certain diseases. For example, somatic mutations in AKT1 have been found in a subset of human cancers, such as breast, ovarian, and colorectal cancers. These mutations can lead to constitutive activation of AKT1, contributing to tumor development. Moreover, germline mutations in AKT1 have been linked to a rare genetic disorder called Proteus syndrome, characterized by asymmetric and progressive overgrowth of various tissues.
Yes, combining AKT1 inhibitors with other therapies is being investigated as a potential strategy for cancer treatment. AKT1 inhibition can enhance the efficacy of conventional chemotherapy agents or targeted therapies. For example, combining AKT1 inhibitors with inhibitors of the phosphoinositide 3-kinase (PI3K)/mTOR pathway, which upstream regulates AKT1, could provide a more comprehensive blockade of the pathway. Additionally, AKT1 inhibitors have also been tested in combination with immune checkpoint inhibitors to enhance immune response against tumors. Such combination approaches aim to improve treatment outcomes and overcome drug resistance mechanisms.
AKT1 signaling regulates numerous downstream targets involved in diverse cellular processes. Some of the well-known targets include the mammalian target of rapamycin (mTOR), which plays a role in protein synthesis and cell growth, and the pro-apoptotic protein Bad, which AKT1 phosphorylates to prevent apoptosis. AKT1 also phosphorylates and inactivates the transcription factor Forkhead box protein O (FOXO), which regulates genes involved in apoptosis, cell cycle arrest, and oxidative stress response. Other downstream targets of AKT1 include glycogen synthase kinase 3 (GSK3), nuclear factor-kappa B (NF-kB), and endothelial nitric oxide synthase (eNOS), among others.
Yes, AKT1 protein has the potential to be a therapeutic target for conditions beyond cancer. Due to its role in insulin signaling and glucose metabolism, targeting AKT1 activity could be beneficial in treating metabolic disorders such as type 2 diabetes. Strategies aimed at increasing AKT1 activity and sensitivity to insulin are being explored.
Targeting AKT1 mutations is an active area of research for therapeutic development. Due to the involvement of AKT1 in cancer progression, efforts are being made to develop specific inhibitors that can selectively target mutant AKT1 forms. Clinical trials are being conducted to investigate the efficacy of AKT inhibitors in patients harboring AKT1 mutations in various cancers. However, further research is still needed to fully understand the implications and potential therapeutic strategies for AKT1 mutations.
AKT1 protein is involved in numerous cellular processes. Some of its key functions include promoting cell survival by inhibiting apoptosis (programmed cell death), regulating cell growth and proliferation, and participating in glucose metabolism. It is also involved in the regulation of protein synthesis, cell cycle progression, DNA repair, and cellular migration.
Yes, certain natural compounds and dietary factors have been found to modulate AKT1 activity. For example, resveratrol, a polyphenol found in grapes and red wine, has been shown to inhibit AKT1 signaling and induce apoptosis in cancer cells. Curcumin, a compound found in turmeric, has also been reported to inhibit AKT1 activation and suppress tumor growth.
AKT1 protein is activated by a process called phosphorylation. When growth factor receptors, such as insulin receptors or receptor tyrosine kinases, are stimulated by their ligands, it triggers the activation of phosphoinositide 3-kinase (PI3K). PI3K then converts phosphatidylinositol 4,5-bisphosphate (PIP2) into phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 acts as a second messenger and recruits AKT1 to the cell membrane.
Yes, AKT1 mutations can contribute to drug resistance in cancer treatment. Mutations in AKT1 can lead to constitutive activation of its signaling pathway, rendering cancer cells resistant to targeted therapies that rely on inhibiting AKT1. For example, tumors with activating mutations in AKT1 may not respond to AKT1 inhibitors. Additionally, mutations in AKT1 or its upstream regulators such as PI3K can bypass the inhibitory effects of targeted therapies.
The activity of AKT1 protein is regulated through various mechanisms. In addition to phosphorylation, which activates AKT1, there are several factors that can modulate its activity. One important regulator is phosphatase and tensin homolog (PTEN), which dephosphorylates PIP3 and limits AKT1 activation. Other regulatory proteins, such as protein phosphatase 2A (PP2A) and protein kinase C (PKC), can also influence AKT1 activity by dephosphorylating or phosphorylating AKT1, respectively.
Dysregulation of AKT1 has been associated with various diseases and conditions. Apart from its prominent role in cancer, altered AKT1 signaling has been implicated in metabolic disorders such as diabetes and obesity. Reduced AKT1 activity is observed in insulin resistance, whereby insulin stimulation of AKT1-mediated glucose uptake is impaired. AKT1 dysregulation has also been linked to neurological disorders, including Alzheimer's disease and schizophrenia. Abnormal AKT1 signaling has been implicated in synaptic dysfunction, neuronal survival, and cognitive impairment associated with these conditions. Further research is needed to fully understand the mechanisms and implications of AKT1 dysregulation in these diseases.
Ask a Question for All Akt1 Products
Required fields are marked with *
My Review for All Akt1 Products
Required fields are marked with *
Inquiry Basket