|Sample Size:||30ug for $99, contact us for details|
Data & Images
|Product Name||Anti-AKT2 Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for RAC-beta serine/threonine-protein kinase(AKT2) detection. Tested with WB, IHC-P, IHC-F in Human;Mouse;Rat.|
|Cite This Product||Anti-AKT2 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9043)|
|Replacement Item||This antibody may replace the following items: sc-5270|sc-7127|sc-81436|sc-81148 from Santa Cruz Biotechnology.|
|Validated Species||Human, Mouse, Rat|
*This antibody is predicted to react with the above species based on antigen sequence similarities. Our Boster Guarantee covers the use of this product with the above species.
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and IHC(F).
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human AKT2(454-481aa DRYDSLGLLELDQRTHFPQFSYSASIRE), different from the related mouse sequence by two amino acids, and from the related rat sequence by one amino acid.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20˚C for one year. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||RAC-beta serine/threonine-protein kinase|
|Molecular Weight||55769 MW|
|Protein 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.|
|Tissue Specificity||Expressed in all cell types so far analyzed.|
|Sequence Similarities||Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.|
|Subcellular Localization||Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3.|
|Alternative Names||RAC-beta serine/threonine-protein kinase;188.8.131.52;Protein kinase Akt-2;Protein kinase B beta;PKB beta;RAC-PK-beta;AKT2;|
|Research Areas|||signal transduction|protein phosphorylation|ser / thr kinases|pkb / akt| cancer|serine/threonine kinases| cardiovascular|atherosclerosis|diabetes associated|heart|cardiac metabolism| metabolism|types of disease|diabetes|heart disease||
Background for RAC-beta serine/threonine-protein kinase
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-AKT2 Picoband™ Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Immunohistochemistry(Frozen Section), 0.5-1μg/ml, Mouse, Rat, -|
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat
Western blot, 0.1-0.5μg/ml, Human
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-AKT2 Picoband™ Antibody Images
Click the images to enlarge.
IHC(P): Human Intestinal Cancer Tissue
IHC(P): Human Lung Cancer Tissue
All lanes: Anti-AKT2(PB9043) at 0.5ug/ml
Lane 1: HELA Whole Cell Lysate at 40ug
Lane 2: PANC Whole Cell Lysate at 40ug
Lane 3: A549 Whole Cell Lysate at 40ug
Lane 4: COLO320 Whole Cell Lysate at 40ug
Lane 5: HT1080 Whole Cell Lysate at 40ug
Lane 6: MCF-7 Whole Cell Lysate at 40ug
Predicted bind size: 56KD
Observed bind size: 56KD
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,