Recombinant Phospho-S6 Ribosomal Protein (Ser235, Ser236) Monoclonal Antibody (AN302076L)
-
-
-
- +2
For research use only.
| Verified Samples |
Verified Samples in WB: MCF-7 Verified Samples in IHC: Human breast cancer, Human lung adenocarcinoma Verified Samples in IF: MCF-7, NIH/3T3 |
| Dilution | WB 1:500-1:1000, IHC 1:200-1:1000, IF 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IHC, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Phosphorylated human S6 ribosomal protein (Ser235/236) peptide |
| Abbre | Phospho-S6 Ribosomal Protein (Ser235, Ser236) |
| Synonyms | RPS, OK/SW-cl, RPS6, S6, OK/SW-cl.2 |
| Swissprot | |
| Calculated MW | 29 kDa |
| Observed MW |
32 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 |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Epigenetics and Nuclear Signaling |
| Clone No. | A796 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Ribosomal Protein S6 (RPS6), a highly conserved component of the eukaryotic 40S small ribosomal subunit, functions as a critical regulatory nexus that translates extracellular and intracellular signals into the control of cell growth and proliferation. This activity is tightly governed by the PI3K/Akt/mTOR signaling cascade, a master regulatory pathway that integrates inputs from growth factors and nutrient availability. In response to mitogenic or anabolic stimuli that activate this pathway, the downstream effector kinase p70 S6K1 mediates the hierarchical phosphorylation of RPS6 on a cluster of serine residues located in its C-terminus, with the phosphorylation of the adjacent serines 235 and 236 representing a canonical hallmark of mTORC1 activation. This specific post-translational modification is mechanistically linked to the primary regulatory function of RPS6, which is to facilitate the selective and efficient translation of a specific cohort of messenger RNAs characterized by a 5' terminal oligo-pyrimidine tract (5' TOP). |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
