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Phospho-GSK3 beta (Ser9) Polyclonal Antibody

Cat:E-AB-20886 Citations (4)
Manual MSDS
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Price: $ 399

Price: $ 240

Price: $ 143

Price: $ 73

Size:
200μL 120μL 60μL 20μL
Quantity:
  • Host: Rabbit
  • Reactivity: Human;Mouse;Rat
  • Applications: WB;IHC-p;IF
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Product Details
Verified Samples Verified Samples in WB:293
Verified Samples in IHC:Human colon
Verified Samples in IF:Rat spleen
Dilution

WB 1:500-1:2000, IHC 1:100-1:300, IF 1:100-1:300

Western Blot Operation Guide
Clonality Polyclonal
Immunogen Synthesized peptide derived from human GSK3β around the phosphorylation site of Ser9
Abbre GSK3β (phospho Ser9)
Synonyms Glycogen Synthase Kinase 3 Beta;Glycogen synthase kinase-3 beta;GSK 3 beta;GSK-3 beta;GSK3B;GSK3B;GSK3beta isoform;Serine/threonine-protein kinase GSK3B
Swissprot
Calculated MW 47kDa
Observed MW 48kDa
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. The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.
Tissue Specificity Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney.
Concentration 1 mg/mL
Buffer PBS with 0.02% sodium azide, 0.5% protective protein and 50% glycerol, pH7.4
Purification Method Affinity purification
Research Areas Cancer; Cardiovascular; Metabolism; Neuroscience; Signal Transduction; Stem Cells
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping Biological ice pack at 4 ℃
background Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates MUC1 in breast cancer cells, and decreases the interaction of MUC1 with CTNNB1/beta-catenin. Phosphorylates CTNNB1/beta-catenin. Phosphorylates SNAI1. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Phosphorylates MACF1 and this phosphorylation inhibits the binding of MACF1 to microtubules which is critical for its role in bulge stem cell migration and skin wound repair.