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Phospho-AKT1 (Ser473) Monoclonal Antibody

Cat:E-AB-51038 Citations (1)
Manual MSDS

Price: $ 399

Price: $ 240

Price: $ 143

Price: $ 73

Size:
200μL 120μL 60μL 20μL
Quantity:
  • Host: Mouse
  • Reactivity: Human
  • Applications: WB;IHC-p
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Product Details
Verified Samples Verified Samples in WB:PC-3
Verified Samples in IHC:Human lung carcinoma
Dilution

WB 1:1000-2000, IHC 1:100-200

Western Blot Operation Guide
Clonality Monoclonal
Immunogen Synthetic Peptide of Phospho-Akt (S473)
Abbre Phospho-AKT1 (Ser473)
Synonyms AKT 1;AKT;AKT1;AKT1;MGC99656;PKB;PKB-ALPHA;PRKBA;Protein Kinase B Alpha;Protein kinase B;Proto-oncogene c-Akt;RAC Alpha;RAC;RAC-alpha serine/threonine-protein kinase;RAC-PK-alpha
Swissprot
Observed MW 60kDa
The actual band is not consistent with the expectation.

Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include:

1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein.

2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes.

3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1.

4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids).

5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers.

If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane.

Cellular Localization Cytoplasm. Nucleus. Cell membrane. Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. 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.
Tissue Specificity Expressed in all human cell types so far analyzed. The Tyr-176 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages.
Concentration 1 mg/mL
Buffer PBS with 0.02% sodium azide, 0.5% protective protein and 50% glycerol, pH7.4
Purification Method Protein A purification
Research Areas Cancer; Epigenetics and Nuclear Signaling; Metabolism; Signal Transduction
Clone No. Clone:7F9
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping Biological ice pack at 4 ℃
background The serine-threonine protein kinase AKT1 is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery.