The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Product Form

1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.

Synonyms

CHDS6, Matrix metalloproteinase 3, Matrix metalloproteinase-3, MGC126102, MGC126103, MGC126104, MMP 3, MMP3, MMP3_HUMAN, Proteoglycanase , SL-1, SL1 , STMY, STMY1, STR1, Stromelysin 1, Stromelysin-1, Transin 1, Transin-1

Suitable Secondaries

See all Anti-Rabbit IgG Secondaries →

Disclaimer

This product is for research use only. It is not intended for diagnostic or therapeutic use.

Scientific Validation Data (2)

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Figure 1: Anti-MMP-3 (S453) Antibody (A25266)

For details please refer to datasheet.

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Figure 2: Anti-MMP-3 (S453) Antibody (A25266)

For details please refer to datasheet.

Citations (4)

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(4)

Proteolytic release of the receptor for advanced glycation end products from in vitro and in situ alveolar epithelial cells.

References: Anti-MMP-3 (S453) Antibody (A25266)

Abstract:

Although the receptor for advanced glycation end products (RAGE) has been used as a biological marker of alveolar epithelial cell injury in clinical studies, the mechanism for release of soluble RAGE from lung epithelial cells has not been well studied. Therefore, these studies were designed to determine the mechanism for release of soluble RAGE after lipopolysaccharide (LPS) challenge. For these purposes, alveolar epithelial cells from rat lungs were cultured on Transwell inserts, and LPS was added to the apical side (500 μg/ml) for 16 h on day 7. On day 7, RAGE was expressed predominantly in surfactant protein D-negative cells, and LPS challenge induced release of RAGE into the medium. This response was partially blocked by matrix metalloproteinase (MMP) inhibitors. Transcripts of MMP-3 and MMP-13 were upregulated by LPS, whereas RAGE transcripts did not change. Proteolysis by MMP-3 and MMP-13 resulted in soluble RAGE expression in the bronchoalveolar lavage fluid in the in situ rat lung, and this reaction was inhibited by MMP inhibitors. In human studies, both MMP-3 and -13 antigen levels were significantly correlated with the level of RAGE in pulmonary edema fluid samples. These results support the conclusion that release of RAGE is primarily mediated by proteolytic damage in alveolar epithelial cells in the lung, caused by proteases in acute inflammatory conditions in the distal air spaces.

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Effects of chronic sleep deprivation on the extracellular signal-regulated kinase pathway in the temporomandibular joint of rats.

References: Anti-MMP-3 (S453) Antibody (A25266)

Abstract:

OBJECTIVES:

To examine the possible involvement and regulatory mechanisms of extracellular signal-regulated kinase (ERK) pathway in the temporomandibular joint (TMJ) of rats subjected to chronic sleep deprivation (CSD).

METHODS:

Rats were subjected to CSD using the modified multiple platform method (MMPM). The serum levels of corticosterone (CORT) and adrenocorticotropic hormone (ACTH) were tested and histomorphology and ultrastructure of the TMJ were observed. The ERK and phospho-ERK (p-ERK) expression levels were detected by Western blot analysis, and the MMP-1, MMP-3, and MMP-13 expression levels were detected by real-time quantitative polymerase chain reaction (PCR) and Western blotting.

RESULTS:

The elevated serum CORT and ACTH levels confirmed that the rats were under CSD stress. Hematoxylin and eosin (HE) staining and scanning electron microscopy (SEM) showed pathological alterations in the TMJ following CSD; furthermore, the p-ERK was activated and the mRNA and protein expression levels of MMP-1, MMP-3, and MMP-13 were upregulated after CSD. In the rats administered with the selective ERK inhibitor U0126, decreased tissue destruction was observed. Phospho-ERK activation was visibly blocked and the MMP-1, MMP-3, and MMP-13 mRNA and protein levels were lower than the corresponding levels in the CSD without U0126 group.

CONCLUSION:

These findings indicate that CSD activates the ERK pathway and upregulates the MMP-1, MMP-3, and MMP-13 mRNA and protein levels in the TMJ of rats. Thus, CSD induces ERK pathway activation and causes pathological alterations in the TMJ. ERK may be associated with TMJ destruction by promoting the expression of MMPs.

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Temporary inductions of matrix metalloprotease-3 (MMP-3) expression and cell apoptosis are associated with tendon degeneration or rupture after corticosteroid injection.

References: Anti-MMP-3 (S453) Antibody (A25266)

Abstract:

Corticosteroid injections are widely used to treat enthesopathy and tendinitis, but are also associated with possible side effects, such as tendon degeneration or rupture. However, the mechanism of tendon degeneration or rupture after corticosteroid injection remains controversial. The purpose of this study was to reveal the mechanism of tendon degeneration or rupture after injection of triamcinolone acetonide (TA) or prednisolone (PSL). Forty-two rats were divided into 3 groups: A normal saline injection group (control group), a TA injection group, and a PSL injection group; the normal saline or corticosteroid was injected around the Achilles tendon. One or 3 weeks after injection, the tendons were subjected to biomechanical testing and histological analysis. At 1 week, the biomechanical strength was significantly lower in the corticosteroid groups. Histological analysis, at 1-week post-injection, showed collagen attenuation, increased expression of MMP-3 and apoptotic cells in the corticosteroid groups. The histological changes and biomechanical weaknesses of the tendon were not seen at 3 weeks. These alterations appeared to be involved in tendon degeneration or rupture after corticosteroid injection.

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Effect of advanced oxidation protein products on articular cartilage and synovium in a rabbit osteoarthritis model.

References: Anti-MMP-3 (S453) Antibody (A25266)

Abstract:

OBJECTIVE:

Advanced oxidation protein products (AOPPs), a marker of oxidative stress, are prevalent in many kinds of disorders. Osteoarthritis (OA), mainly resulting from the regression of cartilage, chronic inflammation of the synovium and the subchondral bone remodeling. Although the inflammatory response of AOPPs on fibroblast-like synoviocytes (FLSs) were reported, the effect of AOPPs on cartilage and synovial in vivo remains unclear. Therefore, our study aims to investigate whether AOPPs have an effect on the articular cartilage and synovial in a rabbit model of OA.

METHODS:

OA model were created by anterior cruciate ligament transection and medial meniscus resection (ACLT + MMx). Forty-eight male New Zealand rabbits were randomly divided into 3 groups: sham-operated group, AOPPs/ACLT + MMx group, and phosphate buffered saline (PBS)/ACLT + MMx group. In sham-operated group, the anterior cruciate ligament was just exposed without transection, and then the incision was sutured. Then intra-articular injection of AOPPs or PBS was performed in the other two groups. Through four weeks and eight weeks of treatment, rabbits in each group were sacrificed. Both hind legs were removed. India ink staining and Safranin O and fast green staining were used to evaluate the macroscopic and microscopic cartilage morphology. The protein expression of matrix metalloproteinases (MMP)-3, MMP-13 in synovium was measured by Western blot.

RESULT:

The India ink score and Mankin score of AOPPs/ACLT + MMx group were both higher than the other two groups at the two time points. Western blot have revealed that intra-articular injection of AOPPs upregulated the protein expression of MMP-3 and MMP-13 in synovium.

CONCLUSION:

AOPPs participated in the occurrence and development of OA by upregulating the protein expression of MMP-3 and MMP-13 in synovium.

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