Recombinant Phospho-p38 MAPK (Thr180, Tyr182) Monoclonal Antibody (AN302090L)
For research use only.
| Verified Samples | Verified Samples in WB: Jurkat, EL4.IL-2, PC-12 |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | phosphorylated human p38 MAPK (Thr180/Tyr182) peptide |
| Abbre | Phospho-p38 MAPK (Thr180, Tyr182) |
| Synonyms | PRKM, SAPK, MAPK13, MAPK 13, MAPK-13, PRKM13, SAPK4, p38delta, MAP kinase 13, MAP kinase p38 delta, MGC99536, Mitogen activated protein kinase 13, Mitogen-activated protein kinase 13, Mitogen-activated protein kinase p38 delta, OTTHUMP00000016282, p38 delta, SAPK 4, Stress activated protein kinase 4, Stress-activated protein kinase 4 |
| Swissprot | |
| Calculated MW | 42 kDa |
| Observed MW |
43 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, Cytosol, Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Cell Biology, Signal Transduction |
| Clone No. | A814 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | p38 MAP kinase (MAPK), also called RK or CSBP, is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress. Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses, including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors. MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 and to phosphorylate the transcription factors ATF-2, Max, and MEF2. SB203580 is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27. SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases. |
Other Clones
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Unconjugated
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