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Recombinant Human AKT2 protein, His & T7-tagged

Cat.No. : AKT2-1841H
Product Overview : Recombinant Human AKT2 aa. (Lys142~Ile412 (Accession # P31751)) fused with N-terminal His & T7 tag was produced in E. coli cells.
  • Specification
  • Gene Information
  • Related Products
Source : E. coli
Species : Human
Tag : His & T7
Form : Freeze-dried powder
Molecular Mass : Predicted Molecular Mass: 35.1kDa
Protein length : Lys142~Ile412 (Accession # P31751)
Endotoxin : <1.0EU per 1ug (determined by the LAL method)
Purity : >95%
Characteristic : The isoelectric point is 7.8.
Applications : SDS-PAGE; WB; ELISA; IP.
Stability : The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition.
Storage : Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months.
Storage buffer : Supplied as lyophilized form in PBS, pH7.4, containing 5% sucrose, 0.01% sarcosyl.
Reconstitution : Reconstitute in sterile PBS, pH7.2-pH7.4.
Gene Name : AKT2 AKT serine/threonine kinase 2 [ Homo sapiens (human) ]
Official Symbol : AKT2
Synonyms : AKT2; AKT serine/threonine kinase 2; PKBB; PRKBB; HIHGHH; PKBBETA; RAC-BETA; RAC-beta serine/threonine-protein kinase; PKB beta; RAC-PK-beta; murine thymoma viral (v-akt) homolog-2; protein kinase Akt-2; protein kinase B beta; putative v-akt murine thymoma viral oncoprotein 2; rac protein kinase beta; v-akt murine thymoma viral oncogene homolog 2
Gene ID : 208
mRNA Refseq : NM_001330511.1
Protein Refseq : NP_001317440.1
UniProt ID : P31751

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (10)

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How is AKT2 protein activated? 03/30/2022

AKT2 can be activated through a process called phosphorylation. When growth factors or hormones such as insulin bind to their receptors on the cell surface, it triggers a signaling cascade resulting in the activation of phosphoinositide 3-kinase (PI3K). PI3K produces a lipid product, which recruits AKT2 to the cell membrane. At the membrane, AKT2 undergoes phosphorylation by activating kinases, leading to its full activation. Once activated, AKT2 phosphorylates downstream targets, initiating various cellular responses.

How is AKT2 protein studied in research? 01/11/2022

Researchers use various molecular and cellular techniques to study AKT2 protein and its functions. This includes techniques like Western blotting to detect and quantify AKT2 protein levels, immunofluorescence microscopy to examine its cellular localization, and kinase activity assays to measure its enzymatic activity.

What are some inhibitors or activators of AKT2 protein? 03/11/2021

Several small molecule inhibitors and activators have been developed to modulate AKT2 activity. Some commonly used AKT inhibitors include LY294002, MK-2206, and GSK2141795. These inhibitors block AKT2 phosphorylation and downstream signaling, leading to the inhibition of cell survival and proliferation. On the other hand, some activators of AKT2 include insulin and growth factors like insulin-like growth factor 1 (IGF-1). These molecules activate the insulin signaling pathway and stimulate AKT2 phosphorylation and activity.

Are there any clinical trials targeting AKT2 protein? 01/20/2021

Clinical trials targeting AKT2 are still in the early stages, and most current trials are focused on AKT inhibitors rather than specifically targeting AKT2. These trials aim to evaluate the safety and efficacy of AKT inhibitors in treating various cancers, including breast, lung, and ovarian cancers.

What role does AKT2 play in insulin signaling? 07/25/2020

AKT2 is a critical component of the insulin signaling pathway. Insulin binds to its receptor on cell surfaces, activating the receptor's intracellular domains. This, in turn, triggers the activation of PI3K and subsequent recruitment and activation of AKT2. Activated AKT2 facilitates the translocation of glucose transporter proteins (GLUT4) to the cell membrane, allowing for the uptake of glucose from the bloodstream into the cells. AKT2 also promotes glycogen synthesis and inhibits glucose production, ultimately maintaining glucose homeostasis.

Are there any genetic mutations associated with AKT2? 04/01/2020

Yes, genetic mutations in the AKT2 gene have been identified and linked to human diseases. These mutations can lead to abnormal AKT2 function and contribute to the development of insulin resistance and type 2 diabetes. Some studies have also suggested that AKT2 mutations might play a role in certain cancers, although further research is needed to clarify the significance of these mutations in cancer development.

Can AKT2 protein be targeted for therapeutic purposes? 09/23/2019

Yes, AKT2 is considered a potential therapeutic target for various diseases, particularly those related to glucose metabolism and insulin resistance. Modulating AKT2 activity can help regulate glucose homeostasis and improve insulin sensitivity. Developing drugs that specifically target AKT2 can potentially lead to more effective treatments for conditions like type 2 diabetes and obesity. However, further research is necessary to fully understand the complexities of AKT2 signaling and its potential as a therapeutic target.

What functions does AKT2 protein have in the body? 03/13/2019

AKT2 has several important functions in the body. It plays a key role in insulin signaling and glucose metabolism by promoting the uptake of glucose into cells and regulating its utilization. AKT2 also contributes to cell survival, growth, and proliferation through various intracellular signaling pathways. Additionally, AKT2 is involved in regulating lipid metabolism, protein synthesis, and cell migration.

Can AKT2 protein be detected in biological samples? 07/23/2016

Yes, AKT2 protein can be detected in various biological samples such as tissue lysates, cell cultures, and body fluids. Techniques like Western blotting, immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA) are commonly used to detect and quantify AKT2 protein levels. These methods rely on specific antibodies that recognize and bind to AKT2, allowing for its detection and measurement. Such assays are invaluable in research and clinical settings for understanding AKT2 expression and its potential implications in disease states.

What happens when AKT2 is dysregulated or dysfunctional? 04/17/2016

Dysregulation or dysfunction of AKT2 can have significant implications for cellular processes and overall health. Reduced or impaired AKT2 signaling is associated with insulin resistance, a condition where cells become less responsive to insulin, resulting in elevated blood glucose levels. Insulin resistance can lead to the development of metabolic disorders like type 2 diabetes, obesity, and cardiovascular diseases. Abnormal AKT2 activity has also been linked to cancer, as it can promote uncontrolled cell growth, survival, and resistance to apoptosis.

Customer Reviews (5)

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Reviews
12/04/2021

    the AKT2 protein is highly recommended for its superior performance in ELISA and its utility in protein electron microscopy structure analysis.

    02/19/2020

      Incorporating the AKT2 protein into research endeavors ensures accurate and comprehensive results, bringing us closer to unraveling the complexities of cellular processes.

      06/24/2017

        Its exceptional reliability and compatibility with various research methodologies make it an invaluable asset for scientists seeking to delve into protein-protein interactions, signaling pathways, and structural investigations.

        03/27/2017

          Such attentive support significantly minimizes potential setbacks and facilitates a seamless and efficient experimental process.

          05/27/2016

            Its robust nature and stability make it suitable for imaging studies, providing researchers with a detailed understanding of the protein's structural characteristics.

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