Recombinant Non-Phospho (Active) β-Catenin (Ser33, Ser37, Thr41) Monoclonal Antibody (AN301881L)

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For research use only.
Verified Samples |
Verified Samples in WB: HeLa, HCT-116, C6 Verified Samples in IHC: Human breast cancer, Mouse colon, Rat stomach Verified Samples in IF: HCT-116 |
Dilution | WB 1:500-1:1000, IHC 1:100-1:500, IF 1:50 |
Isotype | IgG, κ |
Host | Rabbit |
Reactivity | Human, Rat, Mouse |
Applications | WB, IHC, IF |
Clonality | Monoclonal;Recombinant |
Immunogen | Recombinant human Non-phospho (Active) β-Catenin (Ser33/37/Thr41) fragment |
Abbre | Non-Phospho (Active) β-Catenin (Ser33, Ser37, Thr41) |
Synonyms | MRD, PRO, Catenin beta, SW-cl, OK/SW-cl, CTNNB, MRD19, armadillo, beta Catenin, CTNNB1, Beta-catenin, Catenin beta-1, OK, SW-cl.35, OK/SW-cl.35, PRO2286, 88kDa, beta 1, Cadherin associated protein, Catenin (cadherin associated protein), Catenin beta 1, CATNB, CHBCAT, CTNB1, DKFZp686D02253, FLJ25606, FLJ37923, OTTHUMP00000162082, OTTHUMP00000165222, OTTHUMP00000165223, OTTHUMP00000209288, OTTHUMP00000209289 |
Swissprot | |
Calculated MW | 85 kDa |
Observed MW |
100 kDa
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, Cytoskeleton, Cell membrane, Centrosome |
Concentration | 1 mg/mL |
Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
Purification Method | Protein A purified |
Research Areas | Signal Transduction, Neuroscience, Stem Cells, Cancer, Cardiovascular |
Clone No. | A593 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | Ice bag |
background | β-catenin is a key downstream effector in the Wnt signaling pathway. It is implicated in two major biological processes in vertebrates: early embryonic development and tumorigenesis. CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β. GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41. Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines.Non-phospho (Active) β-Catenin (Ser33/37/Thr41) Rabbit mAb specifically recognizes β-catenin that is non-phosphorylated at Ser33, Ser33 or Thr41. Non-phospho β-Catenin (Ser33, Ser33 or Thr41) protein is useful as a readout of stabilized β-catenin protein, and therefore functionally active in cell-cell adhesion and mediating transcriptional activity via the canonical Wnt signaling pathway. |
Other Clones
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