MMP-9 Antibody
(Synonyms: MMP9; CLG4B; Matrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB)Based on 2 publication(s) in Google Scholar
MMP-9 Antibody is a Rabbit-derived and non-conjugated IgG polyclonal antibody, targeting to MMP-9.
-
Host:
Rabbit
-
Isotype:
IgG
-
Application:
WB, IHC-P, ICC/IF
-
Reactivity :
Human, Mouse, Rat
-
Formulation:
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
-
Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Publications Citing Use of MedChemExpress (MCE) MMP-9 Antibody
More
Applications
| Application |
WB
WB: Western Blot
|
IHC-P
IHC-P: Immunohistochemistry-Paraffin
|
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:200 |
Product Details
MMP-9 Antibody is a Rabbit-derived and non-conjugated IgG polyclonal antibody, targeting to MMP-9.
-
Host Rabbit
-
Clonality Polyclonal
-
Species ReactivityHuman, Mouse, Rat
-
Observed Molecular WeightObserved band size: 100 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
-
Calculated Molecular Weight Predicted band size: 78 kDa
Synthetic peptide corresponding to Human MMP9.The exact sequence is proprietary to MCE.
Endogenous
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
-
Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
-
Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
-
Shipping
Shipping with blue ice.
Publications (2)
-
Journal Impact Factor
-
Most Recent
-
Adv Sci (Weinh)
2025 Jul;12(25):e2501112. PMID: 40171827
Verification Images
-
Immunohistochemical analysis of paraffin-embedded human Liver Cancer tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Immunohistochemical analysis of paraffin-embedded human Liver Cancer tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Immunohistochemical analysis of paraffin-embedded human Liver Cancer tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Immunohistochemical analysis of paraffin-embedded human Cervical Cancer tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Immunohistochemical analysis of paraffin-embedded human Colon cancer tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Immunohistochemical analysis of paraffin-embedded human cholangiocarcinoma tissue using MMP-9 antibody was performed. The section was pretreated using high-temperature and high-pressure mediated EDTA antigen retrieval buffer (pH 9.0), for 5 minutes. The tissues were incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes. Detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. The tissues were counterstained with hematoxylin and mounted with neutral balsam mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Colon cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Colon cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Colon cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Liver Cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Liver Cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Tyramide signaling amplification based immunofluorescence was performed on paraffin-embedded human Liver Cancer tissue using MMP-9 antibody. Antigen retrieval was performed in EDTA buffer pH 9.0 (95 °C, 20 min) followed by cooling to RT. Then incubated with primary antibody (HY-P80756, 1:5000 dilution) at room temperature for 30 minutes and HRP conjugated secondary antibody for 10 minutes. Fluorescence was then developed with Vari Fluor 532 TSA (200×)（HY-D1832）. The tissues were counterstained with DAPI and mounted with Anti-fade mounting medium. -
Immunocytochemistry analysis of Hela cells labeling MMP-9 with MMP-9 Antibody (HY-P80756) at 1/100 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes at room temperature, then blocked with quick block buffer for 10 minutes at room temperature. Cells were then incubated with MMP-9 Antibody (HY-P80756) at 1/100 dilution in quick block buffer overnight at 4 ℃. AF488-conjugated Goat Anti-Rabbit IgG H&L（HY-P8002, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue). -
Immunocytochemistry analysis of U2OS cells labeling MMP-9 with MMP-9 Antibody (HY-P80756) at 1/100 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes at room temperature, then blocked with quick block buffer for 10 minutes at room temperature. Cells were then incubated with MMP-9 Antibody (HY-P80756) at 1/100 dilution in quick block buffer overnight at 4 ℃. AF488-conjugated Goat Anti-Rabbit IgG H&L（HY-P8002, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
Background
-
Function
MMP-9 (matrix metalloproteinase-9)， also known as gelatinase B, is a zinc-dependent extracellular endopeptidase that mediates extracellular matrix remodeling through proteolytic cleavage of gelatin, type IV collagen, laminin, elastin, and additional matrix-associated substrates, thereby regulating tissue turnover, cell migration, and microenvironmental remodeling[1][2]. Mechanistically, MMP-9 is synthesized as an inactive proenzyme and becomes activated through proteolytic removal of its prodomain, enabling participation in inflammatory signaling, leukocyte trafficking, angiogenesis, and tissue repair processes[1][3]. MMP-9 also modulates biological activity of cytokines, chemokines, growth factors, and cell-surface signaling molecules, linking extracellular matrix degradation with immune and vascular responses[3][4]. In disease settings, dysregulated or persistent MMP-9 expression is associated with cancer progression, invasion, metastasis, vascular remodeling, neuroinflammatory disorders, and blood-brain barrier disruption, making MMP-9 a widely studied pathogenic mediator and biomarker candidate[3][5][6]. Compared with the closely related gelatinase MMP-2, MMP-9 displays distinct substrate preferences, inducible expression in inflammatory conditions, predominant storage in neutrophils, and primary inhibition by TIMP-1, whereas MMP-2 is generally constitutively expressed and preferentially regulated by TIMP-2[4]. Structural differences, including a unique loop region and distinct regulatory mechanisms, further support functional separation between the two gelatinases in physiological and pathological remodeling[2][4]. For experimental applications, MMP-9-selective inhibitors and neutralizing antibodies are widely used to investigate extracellular matrix remodeling, angiogenesis, inflammatory responses, and tumor progression, although achieving high selectivity remains a major challenge because of structural homology within the matrix metalloproteinase family[5][7].
-
Subcellular Localization
Secreted, extracellular space, extracellular matrix
-
Expression
Tissue_specificity:Protein levels were detected in neutrophils (PubMed: 7683678) . Produced by normal alveolar macrophages and granulocytes.
Induction:Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells; (Microbial infection) Expression induced by M.bovis MPB83 (at protein level) (PubMed:20800577) -
Subunit
Exists as monomer or homodimer; disulfide-linked (PubMed:1281792, PubMed:7683678). Also exists as heterodimer with LCN2 (PubMed:1281792, PubMed:7683678). Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1 (PubMed:16512877)
-
SwissProt ID
-
Synonyms
MMP9; CLG4B; Matrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB
-
Research Field
Cardiovascular
Documentation
-
Data Sheet (262 KB)
-
SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
-
User Guide for Antibodies (1077 KB)
[1]. Mondal S, et al. Matrix metalloproteinase-9 (MMP-9) and its inhibitors in cancer: A minireview. Eur J Med Chem. 2020 May 15;194:112260. [Content Brief]
[2]. Rashid ZA, et al. Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment. Int J Mol Sci. 2023 Jul 28;24(15):12133. [Content Brief]
[3]. Li H, et al. Matrix Metalloproteinase-9 as an Important Contributor to the Pathophysiology of Depression. Front Neurol. 2022 Mar 18;13:861843. [Content Brief]
[4]. Nikolov A, et al. Role of Gelatinases MMP-2 and MMP-9 in Healthy and Complicated Pregnancy and Their Future Potential as Preeclampsia Biomarkers. Diagnostics (Basel). 2021 Mar 9;11(3):480. [Content Brief]
[5]. Huang H. Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances. Sensors (Basel). 2018 Sep 27;18(10):3249. doi: 10.3390/s18103249. PMID: 30262739; PMCID: PMC6211011. et al. Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances. Sensors (Basel). 2018 Sep 27;18(10):3249. [Content Brief]
[6]. Vandooren J, et al. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol. 2013 May-Jun;48(3):222-72. [Content Brief]
[7]. Vandenbroucke RE, et al. Is there new hope for therapeutic matrix metalloproteinase inhibition? Nat Rev Drug Discov. 2014 Dec;13(12):904-27. [Content Brief]
Powered by Bioz
