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Creative Biolabs

Human 1321N1/P2Y6 Stable Cell Line

[CAT#: NCL20120108CR]

P2Y6 Purinergic Receptor Stable Cell Line

Species:
Human
Applications:
GPCR Screening
Cell Types:
Other Cells

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Product Overview

Description

P2Y receptors are one of three families of extracellular receptors for purine and pyrimidine nucleotides involved in purinergic signaling. In heterologous expression systems, recombinant P2Y1, P2Y2, P2Y4, P2Y6 receptors couple to G proteins (mainly Gq) which, in turn, activate intracellular signaling cascades - mainly the phospholipase Cβ (PLCβ) isoform to mobilise intracellular Ca2+ ions. RT-PCR and Northern Blotting studies show a high expression of this receptor in spleen and placenta, followed by kidney, adipose, bone, lung, heart, brain and skeletal muscle.

Cell Types

Other Cells

Applications

GPCR Screening

Research Areas

GPCR; Neural Signal Transduction

Species

Human
Properties

Size

>1x10^6 Cells

Form

Frozen cells

Culture Medium

DMEM, 10% FBS, 250 μg/ml G418

Freeze Medium

45% culture medium, 45% FBS, 10% DMSO

Receptor

P2Y6

Family

P5Y receptor

Strain

1321N1/P2Y6 Cell Line

Cell Purity

>95%

Shipping

Dry ice

Storage

Liquid nitrogen immediately upon delivery

Handling Advice

Avoid inhalation. Avoid contact with eyes, skin, and clothing. Avoid prolonged or
repeated exposure.

Research Use Only

For research use only, not for diagnostic or therapeutic use.

Warnings

Store under recommended storage conditions (liquid nitrogen). Do not expose to high temperature. After expiration, discard all remaining reagents.
Target Details

Target

P2Y6

Official Name

P2Y6

Alternative Names

P2Y purinoceptor 6; P2RY6; 2010204J23Rik

Gene ID

5031(Human)

Uniprot ID

Q15077(Human)
References

1. Ramírez, M. P., Rivera, M., Quiroga-Roger, D., Bustamante, A., Vega, M., Baez, M.,.. & Wilson, C. A. (2017). Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding. Protein Science, 26(7), 1404-1412. 2. Wang, I., Chen, S. Y., & Hsu, S. T. D. (2015). Unraveling the folding mechanism of the smallest knotted protein, MJ0366. The Journal of Physical Chemistry B, 119(12), 4359-4370.
Publications

Publications (0)

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