GNAS Blocking Peptide (N-Term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P63092 |
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Gene ID | 2778 |
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Other Names | Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Adenylate cyclase-stimulating G alpha protein, GNAS, GNAS1, GSP |
Target/Specificity | The synthetic peptide sequence is selected from aa 71-83 of HUMAN GNAS |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | GNAS |
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Synonyms | GNAS1, GSP |
Function | Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein- coupled receptors (GPCRs) (PubMed:17110384). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:26206488, PubMed:8702665). GNAS functions downstream of several GPCRs, including beta-adrenergic receptors (PubMed:21488135). Stimulates the Ras signaling pathway via RAPGEF2 (PubMed:12391161). |
Cellular Location | Cell membrane {ECO:0000250|UniProtKB:P63094}; Lipid-anchor {ECO:0000250|UniProtKB:P63094} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. Stimulates the Ras signaling pathway via RAPGEF2.
References
Mattera R.,et al.FEBS Lett. 206:36-42(1986).
Harris B.A.,et al.Nucleic Acids Res. 16:3585-3585(1988).
Kozasa T.,et al.Proc. Natl. Acad. Sci. U.S.A. 85:2081-2085(1988).
Puhl H.L. III,et al.Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
Kalnine N.,et al.Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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