Abscisic acid receptor PYL1 Recombinant Protein | PYL1 recombinant protein

Recombinant Arabidopsis thaliana Abscisic acid receptor PYL1

Cat. Num. AAA1265119

• Gene Names: PYL1; MZA15.21; MZA15_21; PYL1; PYR1-like 1; RCAR12; regulatory components of ABA receptor 12
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Abscisic acid receptor PYL1; Recombinant Arabidopsis thaliana Abscisic acid receptor PYL1; ABI1-binding protein 6PYR1-like protein 1; Regulatory components of ABA receptor 9; PYL1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 8-221aa; Partial
• Sequence: SSPVNEEENSQRISTLHHQTMPSDLTQDEFTQLSQSIAEFHTYQLGNGRCSSLLAQRIHAPPETVWSVVRRFDRPQIYKHFIKSCNVSEDFEMRVGCTRDVNVISGLPANTSRERLDLLDDDRRVTGFSITGGEHRLRNYKSVTTVHRFEKEEEEERIWTVVLESYVVDVPEGNSEEDTRLFADTVIRLNLQKLASITEAMNRNNNNNNSSQVR
• Sequence Length: 221

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for PYL1 recombinant protein

Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.

Product Categories/Family for PYL1 recombinant protein

Neuroscience

References

Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones.Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.DNA Res. 5:379-391(1998) The Arabidopsis Information Resource (TAIR) Empirical analysis of transcriptional activity in the Arabidopsis genome.Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.Science 302:842-846(2003) PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-interacting proteins in Arabidopsis.Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.Plant J. 61:290-299(2010) Regulators of PP2C phosphatase activity function as abscisic acid sensors.Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., Grill E.Science 324:1064-1068(2009) Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins.Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y., Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P., Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.Science 324:1068-1071(2009) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors.Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M., Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J., Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F., Cutler S.R., Zhu J.-K., Xu H.E.Nature 462:602-608(2009) Structural basis of abscisic acid signalling.Miyazono K.-I., Miyakawa T., Sawano Y., Kubota K., Kang H.-J., Asano A., Miyauchi Y., Takahashi M., Zhi Y., Fujita Y., Yoshida T., Kodaira K.-S., Yamaguchi-Shinozaki K., Tanokura M.Nature 462:609-614(2009) Structural insights into the mechanism of abscisic acid signaling by PYL proteins.Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J., Yan N.Nat. Struct. Mol. Biol. 16:1230-1236(2009)

NCBI and Uniprot Product Information

• NCBI GI #: 22327625
• NCBI GeneID: 834722
• NCBI Accession #: NP_199491.2
• NCBI GenBank Nucleotide #: NM_124049.4
• UniProt Accession #: Q8VZS8; Q9FIP6
• Molecular Weight: 28.7 kDa
• NCBI Official Full Name: abscisic acid receptor PYL1
• NCBI Official Symbol: PYL1
• NCBI Official Synonym Symbols: MZA15.21; MZA15_21; PYL1; PYR1-like 1; RCAR12; regulatory components of ABA receptor 12
• NCBI Protein Information: abscisic acid receptor PYL1
• UniProt Protein Name: Abscisic acid receptor PYL1
• Protein Family: Abscisic acid receptor
• UniProt Gene Name: PYL1
• UniProt Synonym Gene Names: RCAR12
• UniProt Entry Name: PYL1_ARATH

Uniprot Description

Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA (PubMed:19407143, PubMed:19855379, PubMed:19893533, PubMed:19898420, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).