- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
MMP9 Antibody / Matrix metalloproteinase-9 [clone SPM425] (V8238)
Email: info@nsjbio.com
| Catalog No | Formulation | Size | Price (USD) | ||
|---|---|---|---|---|---|
|
V8238-100UG | 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide | 100 ug | 559 | |
|
|
V8238-20UG | 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide | 20 ug | 259 | |
|
|
V8238SAF-100UG | 1 mg/ml in 1X PBS; BSA free, sodium azide free | 100 ug | 559 |
|
| Availability | 1-3 business days |
| Species Reactivity | Human |
| Format | Purified |
| Host | Mouse |
| Clonality | Monoclonal (mouse origin) |
| Isotype | Mouse IgG2b, kappa |
| Clone Name | SPM425 |
| Purity | Protein G affinity chromatography |
| UniProt | P14780 |
| Localization | Cytoplasmic, nuclear, secreted |
| Applications | Immunohistochemistry (FFPE) : 1-2ug/ml |
| Limitations | This MMP9 antibody is available for research use only. |
|
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MMP9 antibody targets Matrix metalloproteinase-9, a secreted zinc-dependent endopeptidase encoded by the human MMP9 gene and a member of the matrix metalloproteinase family. Matrix metalloproteinase-9, also widely referred to as MMP-9 and gelatinase B in the literature, is primarily localized to the extracellular space where it degrades components of the extracellular matrix. MMP9 antibody is frequently used in studies investigating tissue remodeling, inflammation, angiogenesis, and tumor invasion due to the enzyme's well-established role in extracellular matrix degradation.
MMP9 is synthesized as a proenzyme that requires proteolytic activation to become catalytically active. It efficiently cleaves type IV collagen, gelatin, elastin, and other basement membrane components, thereby facilitating cell migration and tissue restructuring. Gelatinase B activity is tightly regulated by tissue inhibitors of metalloproteinases, particularly TIMP1, to maintain extracellular matrix balance. Dysregulated MMP9 expression has been implicated in cancer metastasis, chronic inflammatory diseases, cardiovascular remodeling, and neurological disorders. MMP9 antibody is therefore valuable for evaluating proteolytic activity in both physiological and pathological contexts.
MMP9 is expressed in neutrophils, macrophages, endothelial cells, and various tumor cells, especially under inflammatory stimulation. In oncology research, elevated Matrix metalloproteinase-9 levels are associated with increased tumor invasiveness and poor prognosis in multiple cancer types. Beyond cancer biology, MMP-9 also contributes to wound healing, blood-brain barrier permeability, and immune cell trafficking.
Structurally, Matrix metalloproteinase-9 contains a signal peptide, a propeptide domain, a catalytic zinc-binding domain, fibronectin type II repeats that enhance gelatin binding, and a hemopexin-like domain involved in substrate specificity. An MMP9 antibody is suitable for detecting Matrix metalloproteinase-9 expression in inflammation, extracellular matrix remodeling, and tumor progression research applications.
Optimal dilution of the MMP9 antibody should be determined by the researcher.
A recombinant human partial protein (amino acids 22-166) was used as the immunogen for this MMP9 antibody.
Store the MMP9 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
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