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For research use only.

Verified Samples Verified Samples in WB: HepG2, 293T, Hela, AD293T, Hela
Dilution WB 1:500-1:2000,  IHC 1:100-1:300,  IF 1:200-1:1000
Isotype IgG
Host Rabbit
Reactivity Human,  Mouse,  Rat
Applications WB,  IHC-p,  IF
Clonality Polyclonal
Immunogen Synthesized peptide derived from human p53 around the acetylation site of K381
Abbre p53 (Acetyl Lys381)
Synonyms Antigen NY-CO-13,  BCC7,  Cellular tumor antigen p53,  FLJ92943,  LFS1,  Mutant tumor protein 53,  P53,  Phosphoprotein p53,  TRP53,  Tp53,  Transformation related protein 53,  Tumor protein 53,  Tumor protein p53,  Tumor suppressor p53,  p53,  p53 tumor suppressor
Swissprot
Calculated MW 44 kDa
Observed MW 53 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, Cytoplasm, Nucleus, Nucleus>PML body, Endoplasmic reticulum, Interaction with BANP promotes nuclear localization, Recruited into PML bodies together with CHEK2, Nucleus, Cytoplasm, Localized in both nucleus and cytoplasm in most cells, In some cells, forms foci in the nucleus that are different from nucleoli, Nucleus, Cytoplasm, Localized in the nucleus in most cells but found in the cytoplasm in some cells, Nucleus, Cytoplasm, Localized mainly in the nucleus with minor staining in the cytoplasm, Nucleus, Cytoplasm, Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4 and Nucleus, Cytoplasm, Predominantly nuclear but translocates to the cytoplasm following cell stress.
Tissue Specificity Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.
Concentration 1 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol.
Purification Method Affinity purification
Research Areas Cancer,  Cell Biology,  Epigenetics and Nuclear Signaling
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended.
background The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p kinase, which acts upstream of the stress-induced mitogen-activated protein kinase cascade. The encoded protein can phosphorylate myelin basic protein and undergoes autophosphorylation. A caspase-cleaved fragment of the encoded protein has been shown to be capable of phosphorylating histone H2B. The particular phosphorylation catalyzed by this protein has been correlated with apoptosis, and it's possible that this protein induces the chromatin condensation observed in this process.
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Unconjugated

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