Recombinant Pim-1 Monoclonal Antibody (AN302025L)
For research use only.
| Verified Samples | Verified Samples in WB: K562,?NK-92, TF-1, Raji |
| Dilution | WB 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | Pim-1 |
| Synonyms | PIM, PIM1, Oncogene PIM 1, Oncogene PIM1, PIM 1, Pim 1 kinase, pim 1 kinase 44 kDa isoform, Pim 1 oncogene, pim 1 oncogene (proviral integration site 1), pim1 kinase 44 kDa isoform, Pim2, PIM3, Proto oncogene serine/threonine protein kinase Pim 1, Proto-oncogene serine/threonine-protein kinase Pim-1, Proviral integration site 1, Proviral integration site 2 |
| Swissprot | |
| Calculated MW | 36 kDa |
| Observed MW |
33, 34 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, Membrane |
| 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, Stem Cells, Epigenetics and Nuclear Signaling, Cancer |
| Clone No. | A745 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Pim proteins (Pim-1, Pim-2 and Pim-3) are oncogene-encoded serine/threonine kinases. Pim-1, a serine/threonine kinase highly expressed in hematopoietic cells, plays a critical role in the transduction of mitogenic signals and is rapidly induced by a variety of growth factors and cytokines. Pim-1 cooperates with c-Myc in lymphoid cell transformation and protects cells from growth factor withdrawal and genotoxic stress-induced apoptosis. Pim-1 also enhances the transcriptional activity of c-Myb through direct phosphorylation within the c-Myb DNA binding domain as well as phosphorylation of the transcriptional coactivator p100. Hypermutations of the Pim-1 gene are found in B-cell diffuse large cell lymphomas. Phosphorylation of Pim-1 at Tyr218 by Etk occurs following IL-6 stimulation and correlates with an increase in Pim-1 activity. Various Pim substrates have been identified; Bad is phosphorylated by both Pim-1 and Pim-2 at Ser112 and this phosphorylation reverses Bad-induced cell apoptosis.The corresponding pim-1 gene encodes a pair of proteins through use of different translation initiation sites. Both larger 44 kDa (Pim-1L) and smaller 33 kDa (Pim-1S) proteins are active kinases, but differ in stability. |
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