| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Heat shock 70 kDa protein 1A|Heat shock 70 kDa protein 1|HSP70-1; HSP70.1|HSPA1A|HSP72|HSPA1|HSX70 |
| Assay Time | |
| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Sensitivity | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Background
human HSP72 (Heat Shock Protein 72) (70) is a molecular target commonly studied in neuroscience, cancer, and immunology 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 HSP72 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 HSP72 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
HSP72 (Heat Shock Protein 72) (70) may also be referenced as Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1, and HSP70-1 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 HSP72 relates to neuronal signaling and synaptic function, neuroinflammation, neurodegeneration models, and brain–body communication in neuroscience, cancer, and immunology research.
- Interpreting shifts in HSP72 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
HSP72 has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with neuroscience, cancer, and immunology 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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Association of Elevated Extracellular HSP72 in Albuminuria with Systemic Inflammation and Disease Progression in Type 2 Diabetic Kidney Disease
IF: 2.8 Journal: Clinical Biochemistry Author: Department of Biochemistry, Jawaharlal Institute of Postgraduate Medical Education and Research (JIPMER), Puducherry, India Cited Date: 2023-11-17