- Antibody Type
- Recombinant monoclonal
- Target
- Phospho-S6 Ribosomal Protein (Ser235/Ser236)
- Reactivity
- Human, Mouse
- Application
- WB,ICC/IF
- MW(Calculated)
- 32kDa
- MW(Observed)
- 32kDa
- Host Species
- Rabbit
- Isotype
- IgG
- Conjugate
- Unconjugated
- Modification
- Phosphorylation
- Modification Site
- Ser235/Ser236
- Recommended dilution ratio
- WB 1:500-1000;ICC/IF 1:100-300
- Composition
- PBS, Glycerol, BSA
- Purification process
- Protein A
- storageCondition
- Store at -20°C. Avoid repeated freeze-thaw cycles
- Stability
- Stable for 12 months from date of receipt / reconstitution.
- Concentration
- --
- Clonal
- Recombinant monoclonal
- Clone Number
- W-R29
- Immunogen
- polypeptide
- Gene Name
- RPS6
- Protein Name
- 40S ribosomal protein S6
- Alternative name
- RPS6, RS6, S6
- Organism-1
- Human
- Gene ID
- 6194
- SwissProt-1
- P62753
- --
- Background:
- Background
- Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions. These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation. Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy terminal region of S6 protein.
- Cellular Localization
- Cytoplasm, Nucleus
- --
- Background:Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions. These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation. Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy terminal region of S6 protein.
- --
- --
- --
- --
- --
- --
- --
- --
- --
- --
- --
- --