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β2-Adrenoceptor Antibodies

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Agonist-induced Serine355/Serine356 phosphorylation of the β2 Adrenoceptor
pS355/pS356-β2 (phospho-β2-Adrenoceptor Antibody)
Serine355/Serine356 (S355/S356) is a major phosphorylation site of the β2 adrenoceptor. The pS355/pS356-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S355/S356...
$ 375.00 *
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Citations
NEW
Agonist-induced Threonine360/Serine364 phosphorylation of the β2 Adrenoceptor
pT360/pS364-β2 (phospho-β2-Adrenoceptor Antibody)
Threonine360/Serine364 (T360/S364) is a major phosphorylation site of the β2 adrenoceptor. The pT360/pS364-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. T360/S364...
$ 375.00 *
Details
NEW
Agonist-induced Serine355 phosphorylation of the β2-Adrenoceptor
pS355-β2 (phospho-β2-Adrenoceptor Antibody)
Serine355 (S355) is a major phosphorylation site of the β2 adrenoceptor. The pS355-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S355 phosphorylation is primarily...
$ 375.00 *
Details
NEW
Agonist-induced Serine356 phosphorylation of the β2-Adrenoceptor
pS356-β2 (phospho-β2-Adrenoceptor Antibody)
Serine356 (S356) is a major phosphorylation site of the β2 adrenoceptor. The pS356-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S356 phosphorylation is primarily...
$ 375.00 *
Details
NEW
Agonist-induced Serine364 phosphorylation of the β2-Adrenoceptor
pS364-β2 (phospho-β2-Adrenoceptor Antibody)
Serine364 (S364) is a major phosphorylation site of the β2 adrenoceptor. The pS364-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S364 phosphorylation is primarily...
$ 375.00 *
Details
NEW
Validation of the β2-Adrenoceptor in transfected HEK293 cells
β2 (non-phospho), β2-Adrenoceptor Antibody
The non-phospho- β2 antibody is directed against the third intracellular loop of human β2 . It can be used to detect total β2 receptors in Western blots independent of phosphorylation. The non-phospho- β2 antibody can also be used to...
$ 375.00 *
Details
NEW
Agonist-induced Serine261/Serine262 phosphorylation of the β2-Adrenoceptor
pS261pS262-β2 (phospho-β2-Adrenoceptor Antibody)
Serine261/Serine262 (S261/S262) is a major phosphorylation site of the β2 adrenoceptor. The pS261/pS262-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S261/S262...
$ 375.00 *
Details
SAMPLE PACK
Agonist-induced Serine355/Serine356 phosphorylation of the β2-Adrenoceptor
β2-Adrenoceptor Sample Pack (phospho- and...
β2-Adrenoceptor Antibody Sample Pack consisting of three phospho- and one non-phospho-β2-Adrenoceptor Antibodies 4 x 20 µL trial size each. Specifically, this sample pack contains the following antibodies pS355/pS356-β2 (7TM0029A),...
$ 300.00 *
Details
NEW
Agonist-induced Threonine360 phosphorylation of the β2-Adrenoceptor
pT360-β2 (phospho-β2-Adrenoceptor Antibody)
Threonine360 (T360) is a major phosphorylation site of the β2 adrenoceptor. The pT360-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. T360 phosphorylation is primarily...
$ 350.00 *
Details

The β2-adrenoceptor is responsible for relaxation of vascular, uterine, and airway smooth muscle. The β2-adrenoceptor is much less sensitive to noradrenaline then to adrenaline. Many potent and selective β2-adrenoceptor agonists have been developed, which are used in the treatment of asthma. β2-adrenoceptor desensitization, β-arrestin recruitment and internalization are regulated by phosphorylation of serine261/serine262 (pS261/pS262-ß2) in the third intracellular loop and carboxyl-terminal serine355/serine356 (pS355/pS356-ß2) and threonine360/serine364 (pT360/pS364-ß2) residues. Agonist-induced phosphorylation of S261/S262 is predominantly mediated by PKA. Agonist-induced phosphorylation of S355/S356 is predominantly mediated by GRK5/6, whereas phosphorylation of T360/S364 is predominantly mediated by GRK2/3. This nomenclature refers to the human β2. For more information on β2-adrenoceptor pharmacology please refer to the IUPHAR database. For further reading refer to:

Nobles KN, Xiao K, Ahn S, Shukla AK, Lam CM, Rajagopal S, Strachan RT, Huang TY, Bressler EA, Hara MR, Shenoy SK, Gygi SP, Lefkowitz RJ. Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Sci Signal. 2011 Aug 9;4(185):ra51. doi: 10.1126/scisignal.2001707. PMID: 21868357; PMCID: PMC3415961.

Kobilka BK. Structural insights into adrenergic receptor function and pharmacology. Trends Pharmacol Sci. 2011 Apr;32(4):213-8. doi: 10.1016/j.tips.2011.02.005. Epub 2011 Mar 15. PMID: 21414670; PMCID: PMC3090711.

The β2-adrenoceptor is responsible for relaxation of vascular, uterine, and airway smooth muscle. The β2-adrenoceptor is much less sensitive to noradrenaline then to adrenaline. Many potent... read more »
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β2-Adrenoceptor Antibodies

The β2-adrenoceptor is responsible for relaxation of vascular, uterine, and airway smooth muscle. The β2-adrenoceptor is much less sensitive to noradrenaline then to adrenaline. Many potent and selective β2-adrenoceptor agonists have been developed, which are used in the treatment of asthma. β2-adrenoceptor desensitization, β-arrestin recruitment and internalization are regulated by phosphorylation of serine261/serine262 (pS261/pS262-ß2) in the third intracellular loop and carboxyl-terminal serine355/serine356 (pS355/pS356-ß2) and threonine360/serine364 (pT360/pS364-ß2) residues. Agonist-induced phosphorylation of S261/S262 is predominantly mediated by PKA. Agonist-induced phosphorylation of S355/S356 is predominantly mediated by GRK5/6, whereas phosphorylation of T360/S364 is predominantly mediated by GRK2/3. This nomenclature refers to the human β2. For more information on β2-adrenoceptor pharmacology please refer to the IUPHAR database. For further reading refer to:

Nobles KN, Xiao K, Ahn S, Shukla AK, Lam CM, Rajagopal S, Strachan RT, Huang TY, Bressler EA, Hara MR, Shenoy SK, Gygi SP, Lefkowitz RJ. Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Sci Signal. 2011 Aug 9;4(185):ra51. doi: 10.1126/scisignal.2001707. PMID: 21868357; PMCID: PMC3415961.

Kobilka BK. Structural insights into adrenergic receptor function and pharmacology. Trends Pharmacol Sci. 2011 Apr;32(4):213-8. doi: 10.1016/j.tips.2011.02.005. Epub 2011 Mar 15. PMID: 21414670; PMCID: PMC3090711.

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