Host: |
Rabbit |
Applications: |
WB |
Reactivity: |
Human/Mouse/Rat |
Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Short Description: |
Rabbit polyclonal antibody anti-Phospho-c-Fos-T232 is suitable for use in Western Blot research applications. |
Clonality: |
Polyclonal |
Conjugation: |
Unconjugated |
Isotype: |
IgG |
Formulation: |
PBS with 0.02% Sodium Azide, 50% Glycerol, pH7.3. |
Purification: |
Affinity purification |
Dilution Range: |
WB 1:500-1:2000 |
Storage Instruction: |
Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Gene Symbol: |
FOS |
Gene ID: |
2353 |
Uniprot ID: |
FOS_HUMAN |
Immunogen: |
A synthetic phosphorylated peptide around T232 of human c-Fos (NP_005243.1). |
Immunogen Sequence: |
VATPE |
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. |
Protein Name | Protein C-FosCellular Oncogene FosFos Proto-Oncogene - Ap-1 Transcription Factor SubunitG0/G1 Switch Regulatory Protein 7Proto-Oncogene C-FosTranscription Factor Ap-1 Subunit C-Fos |
Database Links | Reactome: R-HSA-2559580Reactome: R-HSA-2559582Reactome: R-HSA-2871796Reactome: R-HSA-450341Reactome: R-HSA-6785807Reactome: R-HSA-6796648Reactome: R-HSA-9018519Reactome: R-HSA-9031628Reactome: R-HSA-9634638Reactome: R-HSA-9768919 |
Cellular Localisation | NucleusEndoplasmic ReticulumCytoplasmCytosolIn Quiescent CellsPresent In Very Small Amounts In The CytosolFollowing Induction Of Cell GrowthFirst Localizes To The Endoplasmic Reticulum And Only Later To The NucleusLocalization At The Endoplasmic Reticulum Requires Dephosphorylation At Tyr-10 And Tyr-30 |
Alternative Antibody Names | Anti-Protein C-Fos antibodyAnti-Cellular Oncogene Fos antibodyAnti-Fos Proto-Oncogene - Ap-1 Transcription Factor Subunit antibodyAnti-G0/G1 Switch Regulatory Protein 7 antibodyAnti-Proto-Oncogene C-Fos antibodyAnti-Transcription Factor Ap-1 Subunit C-Fos antibodyAnti-FOS antibodyAnti-G0S7 antibody |
Information sourced from Uniprot.org
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