|Validated Species:||Chicken, Human, Mouse, Rat|
Data & Images
|Product Name||Anti-PKB Alpha Antibody (Monoclonal, PKB-175)|
|Description||Mouse IgG monoclonal antibody for PKB alpha, v-akt murine thymoma viral oncogene homolog 1 (AKT1) detection. Tested with WB in Human;mouse;rat;chicken. No cross reactivity with other proteins.|
|Cite This Product||Anti-PKB Alpha Antibody (Monoclonal, PKB-175) PKB-175 (Boster Biological Technology, Pleasanton CA, USA, Catalog # MA1085)|
|Replacement Item||This antibody may replace the following items: sc-271149|sc-1618|sc-5298|sc-55523|sc-7126|sc-377457|sc-135829|sc-1618-R from Santa Cruz Biotechnology.|
|Validated Species||Chicken, 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-Mouse IgG (EK1001) for Western blot.
*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 2018!
|Immunogen||Synthetic peptide corresponding to amino acids 461-477 of human PKB alpha/Akt1, conjugated to KLH.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Mouse ascites fluid, 1.2% sodium acetate, 2mg BSA, with 0.01mg NaN3 as preservative.|
|Concentration||Add 1ml of PBS buffer will yield a concentration of 100ug/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.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||RAC-alpha serine/threonine-protein kinase|
|Molecular Weight||55735 MW|
|Protein Function||AKT1 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. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr- 117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation (By similarity). Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity (By similarity). Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53 (By similarity). .|
|Tissue Specificity||Widely expressed. Low levels found in liver with slightly higher levels present in thymus and testis.|
|Sequence Similarities||Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.|
|Subcellular Localization||Cytoplasm . Nucleus . Cell membrane . Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A (By similarity). Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles (By similarity). .|
|Alternative Names||RAC-alpha serine/threonine-protein kinase;18.104.22.168;Protein kinase B;PKB;Protein kinase B alpha;PKB alpha;RAC-PK-alpha;Akt1;|
|Research Areas|||signal transduction|protein phosphorylation|ser / thr kinases|pkb / akt| epigenetics and nuclear signaling|cell cycle|apoptosis|nuclear| cancer|serine/threonine kinases| metabolism|pathways and processes|metabolism processes|cell death||
Background for RAC-alpha serine/threonine-protein kinase
Anti-PKB Alpha Antibody (Monoclonal, PKB-175) Images
Click the images to enlarge.
All lanes: Anti PKB alpha (MA1085) at 0.5ug/ml
Lane 1: Rat Ovary Tissue Lysate at 50ug
Lane 2: PC-12 Whole Cell Lysate at 40ug
Lane 3: A549 Whole Cell Lysate at 40ug
Lane 4: MCF-7 Whole Cell Lysate at 40ug
Lane 5: HEPA Whole Cell Lysate at 40ug
Predicted bind size: 56KD
Observed bind size: 56KD