PDIL1-1 Antibody

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Description

Definition and Biological Role

PDIL1-1 is a member of the protein disulfide isomerase (PDI) family, which facilitates disulfide bond formation and protein folding in the endoplasmic reticulum (ER). In rice (Oryza sativa), PDIL1-1 specifically regulates the oxidative folding of vacuole-targeted storage proteins such as proglutelins and α-globulin, ensuring proper seed development and nutrient storage . Loss of PDIL1-1 disrupts starch granule formation, increases reactive oxygen species (ROS)-related proteins, and causes irregular protein bodies, leading to chalky endosperm phenotypes .

Applications of PDIL1-1 Antibody

The PDIL1-1 antibody has been utilized in multiple experimental contexts:

Key Applications

  • Western Blotting: Detects PDIL1-1 expression in rice seeds during developmental stages (5–50 days after flowering) .

  • Mutant Analysis: Identifies PDIL1-1Δ knock-out mutants, which exhibit reduced protein content, elevated free sugars, and thickened aleurone layers .

  • Protein Interaction Studies: Confirms PDIL1-1’s interaction with cysteine protease OsCP1, suggesting a role in inhibiting premature programmed cell death (PCD) during seed maturation .

Example Protocol (Western Blot)

StepParameters
Protein Extraction50 mM Tris-Cl (pH 7.5), 150 mM NaCl, 1% Triton X-100, 1 mM PMSF
Electrophoresis10% SDS-polyacrylamide gel
TransferPVDF membrane (Millipore)
DetectionAnti-PDIL1-1 antibody, validated for rice

Functional Insights

  • Seed Phenotype: PDIL1-1Δ mutants show a 20% reduction in total seed protein and a 35% increase in free sugars compared to wild-type seeds .

  • Proteomic Alterations: Loss of PDIL1-1 causes accumulation of glucose/starch metabolism enzymes (e.g., α-amylase) and ROS scavengers (e.g., peroxiredoxin) .

  • Compensatory Mechanisms: PDIL1-1 deficiency upregulates related PDIs (e.g., PDIL2-3), which localize cysteine-rich prolamins but cannot rescue proglutelin misfolding .

Comparative Roles of PDIL Proteins

ProteinFunctionLocalizationMutant Phenotype
PDIL1-1Oxidative folding of proglutelinsER lumenChalky endosperm, thick aleurone
PDIL2-3Prolamin localization in PB-I coresProtein Body-I (PB-I)Heterogeneous PB-I size

Technical Validation

  • Specificity: The anti-PDIL1-1 antibody detects a single band at ~57 kDa in rice seed extracts, with no cross-reactivity to other PDIL isoforms .

  • Developmental Regulation: PDIL1-1 expression peaks at 20–30 days after flowering, coinciding with active storage protein synthesis .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
PDIL1-1 antibody; PDI5 antibody; At1g21750 antibody; F8K7.19 antibody; Protein disulfide isomerase-like 1-1 antibody; AtPDIL1-1 antibody; EC 5.3.4.1 antibody; Protein disulfide-isomerase 1 antibody; PDI 1 antibody; Protein disulfide-isomerase 5 antibody; AtPDI5 antibody
Target Names
PDIL1-1
Uniprot No.

Target Background

Function
Protein disulfide isomerase (PDI5) associates with RD21A protease to facilitate trafficking from the endoplasmic reticulum (ER) through the Golgi apparatus to lytic and protein storage vacuoles of endothelial cells in developing seeds. PDI5 plays a crucial role in regulating the timing of programmed cell death (PCD) of these endothelial cells by chaperoning and inhibiting cysteine proteases during their transport to vacuoles.
Gene References Into Functions
  1. Research indicates that PDI5 is essential for proper seed development and controls the timing of PCD by chaperoning and inhibiting Cys proteases during their trafficking to vacuoles prior to PCD of the endothelial cells. [PDI5] PMID: 18676877
Database Links

KEGG: ath:AT1G21750

STRING: 3702.AT1G21750.1

UniGene: At.24814

Protein Families
Protein disulfide isomerase family
Subcellular Location
Endoplasmic reticulum lumen. Vacuole. Note=Found in protein storage vacuoles and lytic vacuoles in endothelial cells of developing seeds.
Tissue Specificity
Highly expressed in flowers, stems and immature seeds, and at lower levels in leaves and siliques (at protein level).

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