Human NPR1 peptide

Name: Human NPR1 peptide
SKU: DAG-P1736
Rating: 5 (1 reviews)

Synthetic Human NPR1 peptide

COA

SDS

Datasheet

Summary

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.Contains 1 guanylate cyclase domain.Contains 1 protein kinase domain.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Entrez Gene ID

4881

Antigen Description

Guanylyl cyclases, catalyzing the production of cGMP from GTP, are classified as soluble and membrane forms (Garbers and Lowe, 1994 [PubMed 7982997]). The membrane guanylyl cyclases, often termed guanylyl cyclases A through F, form a family of cell-surface receptors with a similar topographic structure: an extracellular ligand-binding domain, a single membrane-spanning domain, and an intracellular region that contains a protein kinase-like domain and a cyclase catalytic domain. GC-A and GC-B function as receptors for natriuretic peptides; they are also referred to as atrial natriuretic peptide receptor A (NPR1) and type B (NPR2; MIM 108961). Also see NPR3 (MIM 108962), which encodes a protein with only the ligand-binding transmembrane and 37-amino acid cytoplasmic domains. NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (ANP (MIM 108780) and BNP (MIM 600295), respectively).[supplied by OMIM, May 2009]

Function

ATP binding; G-protein coupled peptide receptor activity; GTP binding; guanylate cyclase activity; hormone binding; natriuretic peptide receptor activity; peptide hormone binding; protein kinase activity; protein kinase binding;

Synonyms

NPR1; natriuretic peptide receptor 1; ANPa; NPRA; ANPRA; GUC2A; GUCY2A; atrial natriuretic peptide receptor 1; GC-A; ANP-A; NPR-A; ANPR-A; guanylate cyclase A; natriuretic peptide receptor A; atrionatriuretic peptide receptor A; natriuretic peptide A type receptor; atrial natriuretic peptide receptor type A; natriuretic peptide receptor A/guanylate cyclase A (atrionatriuretic peptide receptor A);

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

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References

Expression of Pumpkin CmbHLH87 Gene Improves Powdery Mildew Resistance in Tobacco

FRONTIERS IN PLANT SCIENCE

Authors: Guo, Wei-Li; Chen, Bi-Hua; Guo, Yan-Yan; Chen, Xue-Jin; Li, Qing-Fei; Yang, He-Lian; Li, Xin-Zheng; Zhou, Jun-Guo; Wang, Guang-Yin

Abstract

Powdery mildew (PM), caused by Podosphaera xanthii, is a major threat to the global cucurbit yield. The molecular mechanisms underlying the PM resistance of pumpkin (Cucurbita moschata Duch.) are largely unknown. A homolog of the basic helix-loop-helix (bHLH) transcription factor was previously identified through a transcriptomic analysis of a PM-resistant pumpkin. In this study, this bHLH homolog in pumpkin has been functionally characterized. CmbHLH87 is present in the nucleus. CmbHLH87 expression in the PM-resistant material was considerably downregulated by PM; and abscisic acid, methyl jasmonate, ethephon, and NaCl treatments induced CmbHLH87 expression. Ectopic expression of CmbHLH87 in tobacco plants alleviated the PM symptoms on the leaves, accelerated cell necrosis, and enhanced H2O2 accumulation. The expression levels of PR1a, PR5, and NPR1 were higher in the PM-infected transgenic plants than in PM-infected wild-type plants. Additionally, the chlorosis and yellowing of plant materials were less extensive and the concentration of bacteria at infection sites was lower in the transgenic tobacco plants than in the wild-type plants in response to bacterial wilt and scab pathogens. CmbHLH87 may be useful for genetic engineering of novel pumpkin cultivars in the future.

Knockout ofSlNPR1enhances tomato plants resistance againstBotrytis cinereaby modulatingROShomeostasis andJA/ETsignaling pathways

PHYSIOLOGIA PLANTARUM

Authors: Li, Rui; Wang, Liu; Li, Yujing; Zhao, Ruirui; Zhang, Yuelin; Sheng, Jiping; Ma, Peihua; Shen, Lin

Abstract

Tomato is one of the most popular horticultural crops, and many commercial tomato cultivars are particularly susceptible toBotrytis cinerea.Non-expressor of pathogenesis-related gene 1(NPR1) is a critical component of the plant defense mechanisms. However, our understanding of howSlNPR1influences disease resistance in tomato is still limited. In this study, two independentslnpr1mutants were used to study the role ofSlNPR1in tomato resistance againstB. cinerea. Compared to (WT),slnpr1leaves exhibited enhanced resistance againstB. cinereawith smaller lesion sizes, higher activities of chitinase (CHI), beta-1, 3-glucanases (GLU) and phenylalanine ammonia-lyase (PAL), and significantly increased expressions ofpathogenesis-related genes(PRs). The increased activities of peroxidase (POD), ascorbate peroxidase (APX) and decreased catalase (CAT) activities collectively regulated reactive oxygen species (ROS) homeostasis inslnpr1mutants. The integrity of the cell wall inslnpr1mutants was maintained. Moreover, the enhanced resistance was further reflected by induction of defense genes involved in jasmonic acid (JA) and ethylene (ET) signaling pathways. Taken together, these findings revealed that knocking outSlNPR1resulted in increased activities of defense enzymes, changes in ROS homeostasis and integrity of cell walls, and activation of JA and ET pathways, which confers resistance againstB. cinereain tomato plants.