mProX™ Human TRPC3 Stable Cell Line

Product Information

Target Protein

TRPC3

Target Family

TRPC

Target Protein Species

Human

Host Cell Type

MDA-MB-231; MCF-7; CHO-K1; HEK293

Target Classification

Ion Channel Cell Lines

Target Research Area

CNS Research

Related Diseases

Spinocerebellar Ataxia

Gene ID

7222

UniProt ID

Q13507

Product Properties

Biosafety Level

Level 1

Activity

Yes

Quantity

10⁶ cells per vial

Applications

Through the stimulation of several G-protein-coupled receptors (GPCRs), such as ANG II and endothelin-1 (ET-1) receptors, TRPC3 in VSM has been related to the modulation of vascular tone. As a result, TRPC3 does not appear to affect intrinsic vascular tone, indicating that receptor-mediated artery vasoconstriction may be the mechanism in which TRPC3 is most important for pressure-induced tone. In fact, the mechanism of TRPC3-induced vasoconstriction in cerebral VSM involves IP3-facilitated IP3R and TRPC3 interaction. When TRPC3 is activated, cations such as Na+ and Ca2+ enter the cell, causing membrane depolarization that opens LTCCs and causes vasoconstriction. The customized TRPC3 stable cell line can be used in antibody discovery and development, potential drug candidate screening and signaling pathway researches.

Protocols

Please visit our protocols page.

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FAQ

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Published Data

Fig.1 TRPC3 was over-expressed on the plasma membrane of MDA-MB-231.

Representative confocal pictures of MCF-7 and MDA-MB-231 demonstrating the subcellular localization of TRPC3 (green). TRPC3 antibodies were treated with cells in two separate ways. DAPI was used to label the nuclei (blue). When comparing MDA-MB-231 to MCF-7, merging fluorescence and bright field pictures showed that TRPC3 was overexpressed on the MDA-MB-231 plasma membrane.

Ref: Wang, Yan, et al. "TRPC3 regulates the proliferation and apoptosis resistance of triple negative breast cancer cells through the TRPC3/RASA4/MAPK pathway." Cancers 11.4 (2019): 558.

Pubmed: 31003514

DOI: 10.3390/cancers11040558

Research Highlights

Before the first transmembrane helix, TRPC3 possesses four membrane reentrant helices that resemble elbows. The TRP helix disengages from the pore-lining S6 because it is perpendicular to it, indicating a distinct gating mechanism from other TRP subfamily channels. Remarkably lengthy, the third transmembrane helix S3 forms a distinct transmembrane domain and an extracellular domain that could function as an external stimuli sensor.
Fan, Chen, et al. "Structure of the human lipid-gated cation channel TRPC3." Elife 7 (2018): e36852.
Pubmed: 29726814 DOI: 10.7554/eLife.36852

Two members of the TRPC family, TRPC3 and TRPC6, are abundantly expressed in the heart and have a role in the pathophysiology of heart failure and cardiac hypertrophy, which are pathological reactions to prolonged mechanical stress.
Yamaguchi, Yohei, et al. "Role of TRPC3 and TRPC6 channels in the myocardial response to stretch: Linking physiology and pathophysiology." Progress in biophysics and molecular biology 130 (2017): 264-272.
Pubmed: 28645743 DOI: 10.1016/j.pbiomolbio.2017.06.010