Recombinant Human RAC-beta serine/threonine-protein kinase (AKT2)

SKU:BHP10500316
Overview
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Recombinant AKT2 Human protein produced in E. coli, N-terminal 6xHis-SUMO-tagged spanning 2-481aa. Suitable for binding assays, functional studies, and assay development.
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater
Species Human
Molecular Weight 71.6 kDa
Options selector
Catalog no. Size
CSB-EP001555HU-1MG 1 mg
CSB-EP001555HU-100UG 100 ug
CSB-EP001555HU-20UG 20 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 1 mg, 100 ug, 20 ug
  • Lead time: Made to Order — production begins after purchase. Lead time is typically 13-23 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No CSB-EP001555HU
Activity
  • Not Test
Alternative Names Protein kinase Akt-2;Protein kinase B beta ;PKB beta;RAC-PK-beta
Endotoxin Level Not test
Expression System
  • E. coli
Form Liquid or Lyophilized powder
Function
  • AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1
  • AKT2 and AKT3) called the AKT kinase
  • and which regulate many processes including metabolism
  • proliferation
  • cell survival
  • growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far
  • but for most of them
  • no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins
  • which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9'
  • resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462'
  • thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors)
  • leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular
  • FOXO1 is phosphorylated at 'Thr-24'
  • 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY)
  • thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273'
  • resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318'
  • which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis
  • including correct neuron positioning
  • dendritic development and synapse formation. 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). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; FUNCTION
Molecular Weight 71.6 kDa
Product Type
  • Recombinant Protein
Purity Greater than 90% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # P31751

Scientific Background

AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of th, no isoform specificity has been reported.

Product Description

E. coli Expression

Recombinant Human RAC-beta serine/threonine-protein kinase (AKT2) is a recombinant protein expressed in E. coli and purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Liquid or Lyophilized powder, n-terminal 6xhis-sumo-tagged. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 71.6 kDa
Expression Region 2-481aa
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Form Liquid or Lyophilized powder
Storage Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Endotoxin Level Not test
UniProt Accession P31751
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as N-terminal 6xHis-SUMO-tagged and has been purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Biological activity data are available in the product datasheet. Please contact our support team for activity specifications relevant to your specific application.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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