Recombinant Mouse Stromelysin-1 (MMP3) Protein (His)

Name: Recombinant Mouse Stromelysin-1 (MMP3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03535P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Stromelysin-1 (MMP3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P28862
Target Symbol	MMP3
Synonyms	Mmp3; Stromelysin-1; SL-1; EC 3.4.24.17; EMS-2; Matrix metalloproteinase-3; MMP-3; Transin-1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	PGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAPGPGINGDAHFDDDERWTEDVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTDLSRFHLSQDDVDGIQSLYGTPTASPDVLVVPTKSNSLEPETSPMCSSTLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAFGFLYFFSGSSQLEFDPNAKKVTHILKSNSWFNC
Expression Range	104-477aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.2kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Peptidase M10A family
Database References	KEGG: mmu:17392 STRING: 10090.ENSMUSP00000034497 UniGene: Mm.4993

Gene Functions References

BMAL1 Deficiency Contributes to Mandibular Dysplasia by Upregulating MMP3. PMID: 29276151
MMP3 contributes to the pathogenesis of ARDS by affecting the pulmonary inflammatory response in female mice in relevant models of lung injury. PMID: 27676418
endogenously secreted chemerin plays an autocrine/paracrine role in white adipose tissue, identifying chemerin as a therapeutic target to modulate adipose remodelling. PMID: 27461525
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
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
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
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
Mmp3-knockout mice maintained higher arterial oxygenation compared to wild-type mice in a model of acute lung injury. PMID: 27096327
NMP4 deficiency suppressed the arthritis-induced increase in bone resorption, expression of RANKL and MMP-3 mRNA. PMID: 26378628
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
genetic inactivation of MMP-3 has profound effects on the structural integrity and plasticity response of the visual cortex of adult mice PMID: 24957860
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
Data indicate that interferon regulatory factor-8 (IRF8) regulates tumor behavior in an matrix metalloproteinase 3 (MMP3)-dependent manner. PMID: 26008967
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
These results demonstrated the role of MMP-3 in blood-spinal cord disruption after spinal cord injury for the first time PMID: 25325922
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
Poly(P) induces MMP-3-regulated proliferation and differentiation of induced pluripotent stem cells into odontoblast-like cells. PMID: 25662160
a novel role of MMP3 in nucleus during viral infection PMID: 24416274
an extracellular regulator of the Wnt signaling pathway and mammary stem cell activi PMID: 23871604
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
Elevated expression of MMP-3 in globoid cell leukodystrophy mediates pathophysiological processes in this disease. PMID: 23404611
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
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
the hemopexin domainof MMP3 directs epithelial invasion and branching PMID: 23592797
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
Data indicate significant upregulation of MMP-9 and -3 expressions and activities in stomach with increasing doses and duration of indomethacin. PMID: 22959068
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
Activation of epithelial-mesenchymal transition by MMP-induced expression of Rac1b gave rise to lung adenocarcinoma. PMID: 22786680
MMP-3-triggered Rac1 splicing regulation is modulated by hnRNP A1 PMID: 22345078
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
in vitro and in vivo evidences suggest that MMP-3 plays an inductive role in KIM-1 shedding by PTEC PMID: 22484054
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
Cellular MMP-3 expression was increased by high-dose epinephrine in both skeletal fibroblast and myoblast cell lines. PMID: 21858843
These observations support a novel role for MMP-3 in the pathogenesis of idiopathic pulmonary fibrosis. PMID: 21871427
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
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
MMP-3 is transcriptionally upregulated by Wnt signaling. PMID: 20534975
Concurrent expression of Mmp-3 with many cardiogenic genes reveals a critical role in Noggin-induced cardiac differentiation of embryonic stem cells. PMID: 19138802
analysis of allele-specific regulation of matrix metalloproteinase-3 gene by transcription factor NFkappaB PMID: 20360864
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
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
Matrix metalloproteinase-3 is increased and participates in neuronal apoptotic signaling downstream of caspase-12 during endoplasmic reticulum stress PMID: 20368330
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
EP3 receptor signaling on endothelial cells is essential for the MMP-9 upregulation that enhances tumor metastasis and angiogenesis. PMID: 19799610
COX-2 activity modulates MMP-9 and-3 activities PMID: 19844242
The up-regulation of stromelysin-1 (MMP-3) in a spontaneously demyelinating transgenic mouse precedes onset of disease. PMID: 11830584
Activation of p38 alpha MAPK enhances its expression by mRNA stabilization PMID: 12060661
MMp3 expression correlates with virulence following neurotropic mouse hepatitis virus infection PMID: 12097550
MMP-3 impairs adipose tissue development, possibly by affecting food intake and/or adipose tissue-related angiogenesis PMID: 12669125
MMP-3 induces secondary and tertiary lateral branching of ducts during mid-puberty and early pregnancy. PMID: 12975354

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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