Recombinant Mouse Stromelysin-1 (Mmp3)

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Code CSB-RP175094m
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
Mmp3; Stromelysin-1; SL-1; EC; EMS-2; Matrix metalloproteinase-3; MMP-3; Transin-1
Mus musculus (Mouse)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

The recombinant Mouse Mmp3 was expressed with the amino acid range of 104-477. The theoretical molecular weight of the Mmp3 protein is 46.2 kDa. This Mmp3 protein is produced using e.coli expression system. The Mmp3 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant Mmp3 protein during the following stages.

The mouse Stromelysin-1, encoded by the Mmp3 gene, is a matrix metalloproteinase (MMP) that plays a key role in tissue remodeling and extracellular matrix degradation. It belongs to the zinc-dependent endopeptidase family and is involved in the proteolytic processing of various substrates within the extracellular matrix. Mmp3 is known for its ability to cleave components of the extracellular matrix, such as collagen, fibronectin, and proteoglycans. This activity is crucial for physiological processes like tissue repair, embryonic development, and immune response. Research on mouse Mmp3 spans various areas, including its involvement in arthritis, wound healing, and cancer progression. Understanding the regulation and function of Mmp3 provides insights into its role in normal physiological processes and its potential implications in pathological conditions.

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Target Background

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Gene References into Functions
  1. BMAL1 Deficiency Contributes to Mandibular Dysplasia by Upregulating MMP3. PMID: 29276151
  2. MMP3 contributes to the pathogenesis of ARDS by affecting the pulmonary inflammatory response in female mice in relevant models of lung injury. PMID: 27676418
  3. endogenously secreted chemerin plays an autocrine/paracrine role in white adipose tissue, identifying chemerin as a therapeutic target to modulate adipose remodelling. PMID: 27461525
  4. Overexpression of Mmp3 in 3T3-L1 preadipocytes inhibited differentiation. High fat diet-induced obesity downregulates adipocyte MMP3 expression to trigger adipogenesis, and adipocyte TIMP4 may modulate this process to regulate hyperplastic vs. hypertrophic adipose tissue expansion, fat distribution, and metabolic health in a sex- and depot-dependent manner. PMID: 27879248
  5. Matrix metalloprotease 3 (MMP3), an endogenous neuronal activator of microglia, increased cytokine release from YAC128 microglia compared to wildtype microglia. We found elevated MMP levels in Huntington's Disease (HD) CSF, and MMP levels correlate with disease severity in HD. These data support a novel role for MMPs and microglial activation in HD pathogenesis. PMID: 27033979
  6. These results indicate that periodic induction, via use of an eye drop, of AAV-mediated secretion of MMP-3 into aqueous humour could have therapeutic potential for those cases of glaucoma that are sub-optimally responsive to conventional pressure-reducing medications. PMID: 28158775
  7. Data show that loss of loss of matrix metalloproteinase-3 (MMP-3) repressed the upregulation of the chemokines monocyte chemoattractant protein (MCP)-1 and (C-X-C motif) ligand 1 (CXCL1). PMID: 27809288
  8. Mmp3-knockout mice maintained higher arterial oxygenation compared to wild-type mice in a model of acute lung injury. PMID: 27096327
  9. NMP4 deficiency suppressed the arthritis-induced increase in bone resorption, expression of RANKL and MMP-3 mRNA. PMID: 26378628
  10. MMP-3 produced in blood vessel endothelial cells after spinal cord injury serves as an endogenous molecule for microglial activation followed by p38MAPK activation and proNGF production PMID: 26079709
  11. genetic inactivation of MMP-3 has profound effects on the structural integrity and plasticity response of the visual cortex of adult mice PMID: 24957860
  12. Study suggests that MMP-3 modulates intracellular MAP kinase signaling pathway and as such, influences a molecular chaperone that regulates cytoskeletal components important for neurite outgrowth, neuronal migration and dendritic arborization PMID: 25652596
  13. Data indicate that interferon regulatory factor-8 (IRF8) regulates tumor behavior in an matrix metalloproteinase 3 (MMP3)-dependent manner. PMID: 26008967
  14. Established are novel molecular mechanisms underlying oxidative stress-mediated dopaminergic neuronal death in which MMP3 activation is a key upstream event that leads to Nox1 induction and eventual dopaminergic neuronal death. PMID: 25536219
  15. These results demonstrated the role of MMP-3 in blood-spinal cord disruption after spinal cord injury for the first time PMID: 25325922
  16. study demonstrates that MMP-3 leads to caspase-9 activation and suggests that this occurs indirectly via a cytosolic protein, possibly involving Apaf-1 PMID: 25285627
  17. Poly(P) induces MMP-3-regulated proliferation and differentiation of induced pluripotent stem cells into odontoblast-like cells. PMID: 25662160
  18. a novel role of MMP3 in nucleus during viral infection PMID: 24416274
  19. an extracellular regulator of the Wnt signaling pathway and mammary stem cell activi PMID: 23871604
  20. MMP-3 has a role in nigrostriatal dopaminergic neuronal loss, BBB damage, and neuroinflammation in an MPTP mouse model of Parkinson's disease PMID: 23853428
  21. Elevated expression of MMP-3 in globoid cell leukodystrophy mediates pathophysiological processes in this disease. PMID: 23404611
  22. hnRNP-K regulates extracellular matrix, cell motility, and angiogenesis pathways. Involvement of the selected genes (Cck, Mmp-3, Ptgs2, and Ctgf) and pathways was validated by gene-specific expression analysis PMID: 23564449
  23. These experiments further define the molecular mechanism of estrogen's bone-protective effects by inducing osteoclast apoptosis through upregulation of MMP3 and FasL cleavage. PMID: 22927007
  24. the hemopexin domainof MMP3 directs epithelial invasion and branching PMID: 23592797
  25. These results demonstrate a critical role for MMP3 in motor endplate remodeling, and reveal a potential target for therapeutic intervention to prevent motor endplate degradation following nerve injury. PMID: 23281061
  26. Data indicate significant upregulation of MMP-9 and -3 expressions and activities in stomach with increasing doses and duration of indomethacin. PMID: 22959068
  27. Ras-GRF1 and -GRF2 may act as adaptors that bind PLCgamma1 and restrict Ca2+ signalling to the vicinity of focal adhesions, indicating a new role for these GRFs that is required for IL-1 induction of the Ras-->ERK pathway and MMP-3 expression PMID: 23145787
  28. Activation of epithelial-mesenchymal transition by MMP-induced expression of Rac1b gave rise to lung adenocarcinoma. PMID: 22786680
  29. MMP-3-triggered Rac1 splicing regulation is modulated by hnRNP A1 PMID: 22345078
  30. Developmental and adult cerebellar defects might contribute to the aberrant motor phenotype observed in MMP-3-deficient mice and suggest an involvement of MMP-3 in mouse cerebellar development. PMID: 22108898
  31. in vitro and in vivo evidences suggest that MMP-3 plays an inductive role in KIM-1 shedding by PTEC PMID: 22484054
  32. mRNA levels of MCP-1 and MMP-3 in intervertebral discs significantly diminished and the ability of MCP-1 or MMP-3 expression to respond to TNF-alpha or TWEAK stimulation was significantly reduced as age increased. PMID: 21928379
  33. Cellular MMP-3 expression was increased by high-dose epinephrine in both skeletal fibroblast and myoblast cell lines. PMID: 21858843
  34. These observations support a novel role for MMP-3 in the pathogenesis of idiopathic pulmonary fibrosis. PMID: 21871427
  35. enhanced MMP3 expression by astrocytes in infected MMP9(-/-) mice suggests an active role of resident cells in participating and potentially collaborating with infiltrating cells in regulating blood-brain barrier PMID: 21800363
  36. MMP-3 mediated activation of MMP-9 is required for efficient neointima formation after carotid ligation in vivo and for vascular smooth muscle cell migration in vitro PMID: 21719762
  37. MMP-3 is transcriptionally upregulated by Wnt signaling. PMID: 20534975
  38. Concurrent expression of Mmp-3 with many cardiogenic genes reveals a critical role in Noggin-induced cardiac differentiation of embryonic stem cells. PMID: 19138802
  39. analysis of allele-specific regulation of matrix metalloproteinase-3 gene by transcription factor NFkappaB PMID: 20360864
  40. Early induction of MMP-3 was distinct from MMP-9 during endometriosis, which was regulated by c-Fos and TIMP-3. Melatonin suppressed MMP-3 activity and amplified apoptosis while regressing endometriosis through a caspase-3 mediated pathway. PMID: 20609072
  41. IL-1-induced signaling through focal adhesions leading to MMP3 release and interactions between SHP-2 and PTPalpha are dependent on the integrity of the catalytic domains of PTPalpha. PMID: 20472558
  42. Matrix metalloproteinase-3 is increased and participates in neuronal apoptotic signaling downstream of caspase-12 during endoplasmic reticulum stress PMID: 20368330
  43. These results further indicate a role of MMP-3 in the demise of DArgic neurons and suggest MMP-3 as a candidate cellular target for neuroprotective therapy. PMID: 19815046
  44. EP3 receptor signaling on endothelial cells is essential for the MMP-9 upregulation that enhances tumor metastasis and angiogenesis. PMID: 19799610
  45. COX-2 activity modulates MMP-9 and-3 activities PMID: 19844242
  46. The up-regulation of stromelysin-1 (MMP-3) in a spontaneously demyelinating transgenic mouse precedes onset of disease. PMID: 11830584
  47. Activation of p38 alpha MAPK enhances its expression by mRNA stabilization PMID: 12060661
  48. MMp3 expression correlates with virulence following neurotropic mouse hepatitis virus infection PMID: 12097550
  49. MMP-3 impairs adipose tissue development, possibly by affecting food intake and/or adipose tissue-related angiogenesis PMID: 12669125
  50. MMP-3 induces secondary and tertiary lateral branching of ducts during mid-puberty and early pregnancy. PMID: 12975354

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Subcellular Location
Secreted, extracellular space, extracellular matrix.
Protein Families
Peptidase M10A family
Database Links
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