FOS (Phospho-Thr232) Colorimetric Cell-Based ELISA Kit

The FOS (Phospho-Thr232) Cell-Based ELISA Kit is a convenient, lysate-free, high throughput and sensitive assay kit that can monitor FOS (Phospho-Thr232) protein expression profile in cells. The kit can be used for measuring the relative amounts of FOS (Phospho-Thr232) in cultured cells as well as screening for the effects that various treatments, inhibitors (ie. siRNA or chemicals), or activators have on FOS (Phospho-Thr232) .

Product Specifications

Synonyms

Proto-oncogene c-Fos; Cellular oncogene fos; G0/G1 switch regulatory protein 7; FOS; G0S7

Gene Name

FOS

UniProt

P01100

Reactivity

Human, Mouse, Rat

Applications

ELISA

Detection Range

> 5000 cells/well

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.

Molecular Weight

40695 MW

Shipping Conditions

Available

Storage Conditions

Store at 4°C for up to 6 months.

Product Datasheet

https://www.bosterbio.com/datasheet?sku=EKC2592

Product MSDS

https://www.bosterbio.com/msds?sku=EKC2592

Other Gene Names

Proto-oncogene c-Fos

Subcellular Location

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.