| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Protein disulfide-isomerase A3|58 kDa glucose-regulated protein|58 kDa microsomal protein|p58|Disulfide isomerase ER-60|Endoplasmic reticulum resident protein 57|ER protein 57, ERp57|Endoplasmic reticulum resident protein 60|ER protein 60, ERp60|PDIA3|ERP57|ERP60|GRP58 |
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| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
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| UniProt # |
Background
human PDIA3 (Protein Disulfide Isomerase A3) is a molecular target commonly studied in signal transduction and metabolism research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of PDIA3 is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of PDIA3 can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
PDIA3 (Protein Disulfide Isomerase A3) may also be referenced as Protein disulfide-isomerase A3, 58 kDa glucose-regulated protein, and 58 kDa microsomal protein in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how PDIA3 relates to energy homeostasis, glucose and lipid metabolism, insulin sensitivity and endocrine regulation, and adipose–liver crosstalk in signal transduction and metabolism research.
- Interpreting shifts in PDIA3 levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
PDIA3 has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with signal transduction and metabolism studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
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PDIA3 defines a novel subset of adipose macrophages to exacerbate the development of obesity and metabolic disorders
IF: 27.7 Journal: Cell Metabolism Author: Department of Respiratory and Critical Care Medicine, The Center for Biomedical Research, NHC Key Laboratory of Respiratory Diseases, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China. Cited Date: 2024-09-27
Investigation of endoplasmic reticulum stress-regulated chaperones as biomarkers in idiopathic non-obstructive azoospermia
IF: Journal: Cell Stress and Chaperones Author: Yuksek Ihtisas University, Faculty of Medicine, Department of Medical Biochemistry. Cited Date: 2024-09-06