JNK1/2/3 Polyclonal Antibody (E-AB-31853)
For research use only.
| Verified Samples |
Verified Samples in WB: 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, Chicken |
| Applications | WB, IHC-p, IF |
| Clonality | Polyclonal |
| Immunogen | Synthesized peptide derived from human JNK1/2/3 around the non-phosphorylation site of Thr183. |
| Abbre | JNK1/2/3 |
| Synonyms | JNK-46, JNK1, JNK2, MAP kinase 8, MAPK 8, MAPK8, MAPK9, Mi, Mitogen-activated protein kinase 8, PRKM8, PRKM9, SAPK1, SAPK1A, SAPK1C, SAPK1c, Stress-activated protein kinase 1c, Stress-activated protein kinase JNK1, c-Jun N-terminal kinase 1 |
| Swissprot | |
| Calculated MW | 48 kDa |
| Observed MW |
44 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. |
| 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, Immunology, Signal Transduction |
| 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 | c-Jun N-terminal kinases (JNKs) phosphorylate and augment transcriptional activity of c-Jun. JNKs originate from three genes that yield ten isoforms through alternative mRNA splicing, including JNK1α1,JNK1β1, JNK2α1, JNK2β1 and JNK3α1, which represent the p46 isoforms, and JNK1α2, JNK1β2, JNK2α2, JNK2β2 and JNK3β2, which represent the p54 isoforms. JNKs coordinate cell responses to stress and influence regulation of cell growth and ransformation. The human JNK1 (PRKM8, SAPK1, MAPK8) gene maps to chromosome 10q11.22 and shares 83% amino acid identity with JNK2. JNK1 is necessary for normal activation and differentiation of CD4 helper T (TH) cells into TH1 and TH2 effector cells. Capsaicin activates JNK1 and p38 in Ras-transformed human breast epithelial cells. Nitrogen oxides (NOx) upregulate JNK1 in addition to c-Fos, c-Jun and other signaling kinases, including MEKK1 and p38. |
Other Clones
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Other Formats
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Unconjugated
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