| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Neurosecretory protein VGF|Neuroendocrine regulatory peptide-1|NERP-1|Neuroendocrine regulatory peptide-2|NERP-2|VGF-derived peptide TLQP-21|VGF-derived peptide TLQP-62|Antimicrobial peptide VGF[554-577]|VGF |
| 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 | |
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| Target | |
| UniProt # |
Background
human VGF (Neurosecretory protein VGF) is a molecular target commonly studied in biomedical 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 VGF 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 VGF 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
VGF (Neurosecretory protein VGF) may also be referenced as Neurosecretory protein VGF, Neuroendocrine regulatory peptide-1, and NERP-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 VGF relates to signal transduction, tissue homeostasis, stress responses, and disease-model biology in biomedical research.
- Interpreting shifts in VGF 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
VGF has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with biomedical 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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Neuropeptide precursor vgf promotes neuroendocrine differentiation and cancer-associated fibroblast activation in small cell lung cancer
IF: 16.6 Journal: Cancer Research Author: Guangdong Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, China. Cited Date: 2025-12-05
Neuropeptide Precursor VGF Promotes Liver Metastatic Colonization of Gαq Mutant Uveal Melanoma by Facilitating Tumor Microenvironment via Paracrine Loops
IF: 14.3 Journal: Advanced Science Author: National-Local Joint Engineering Laboratory of Druggability and New Drug Evaluation, Guangdong Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, 510006, China. Cited Date: 2024-10-25
Integrin αVβ1-activated PYK2 promotes the progression of non-small-cell lung cancer via the STAT3-VGF axis
IF: 8.4 Journal: Cell Communication and Signaling Author: Department of Pulmonary and Critical Care Medicine, The First Affiliated Hospital of Soochow University, Suzhou, 215006, China. Cited Date: 2024-06-14