c-Fos Positive Control for STJ506017 peptide (STJ505777)

SKU:
STJ505777-5

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Applications: WB
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: c-Fos Positive Control for STJ506017 is synthetically produced from the sequence and is suitable for use in western blot applications.
Formulation: Provided as 100 uL ready-to-use, in SDS-PAGE sample buffer (Laemelli's buffer) containing Tris, pH 6.8, 1 % SDS, Glycerol and Bromophenolblue blue as tracking dye. The sample is reduced by adding 2% beta mercaptoethanol. The protein concentration is
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: FOS
Gene ID: 2353
Uniprot ID: FOS_HUMAN
Specificity: This is positive control is recommended for use in combination with c-Fos antibody STJ506017.
Immunogen: Purified Proto-oncogene c-Fos.
Post Translational Modifications Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation. Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232. In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis.
Function Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.
Peptide Name Protein C-Fos
Cellular Oncogene Fos
Fos Proto-Oncogene - Ap-1 Transcription Factor Subunit
G0/G1 Switch Regulatory Protein 7
Proto-Oncogene C-Fos
Transcription Factor Ap-1 Subunit C-Fos
Database Links Reactome: R-HSA-2559580
Reactome: R-HSA-2559582
Reactome: R-HSA-2871796
Reactome: R-HSA-450341
Reactome: R-HSA-6785807
Reactome: R-HSA-6796648
Reactome: R-HSA-9018519
Reactome: R-HSA-9031628
Reactome: R-HSA-9634638
Reactome: R-HSA-9768919
Cellular Localisation Nucleus
Endoplasmic Reticulum
Cytoplasm
Cytosol
In Quiescent Cells
Present In Very Small Amounts In The Cytosol
Following Induction Of Cell Growth
First Localizes To The Endoplasmic Reticulum And Only Later To The Nucleus
Localization At The Endoplasmic Reticulum Requires Dephosphorylation At Tyr-10 And Tyr-30
Alternative Peptide Names Protein C-Fos protein
Cellular Oncogene Fos protein
Fos Proto-Oncogene - Ap-1 Transcription Factor Subunit protein
G0/G1 Switch Regulatory Protein 7 protein
Proto-Oncogene C-Fos protein
Transcription Factor Ap-1 Subunit C-Fos protein
FOS protein
G0S7 protein

Information sourced from Uniprot.org

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