Recombinant Mouse Collagenase 3 (MMP13) Protein (His)

Name: Recombinant Mouse Collagenase 3 (MMP13) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02315P
Price: 549.6 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Mmp13.

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

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Product Overview

Description	Recombinant Mouse Collagenase 3 (MMP13) 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	P33435
Target Symbol	MMP13
Synonyms	Mmp13; Collagenase 3; EC 3.4.24.-; Matrix metalloproteinase-13; MMP-13
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	YNVFPRTLKWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSILWC
Expression Range	105-472aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.5kDa
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	Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
Subcellular Location	Secreted, extracellular space, extracellular matrix. Secreted.
Protein Families	Peptidase M10A family
Database References	KEGG: mmu:17386 STRING: 10090.ENSMUSP00000015394 UniGene: Mm.5022
Tissue Specificity	Detected in epidermal cells and stromal fibroblasts in wounded skin, but not in normal skin (at protein level). Detected in embryonic hypertrophic chondrocytes and newly recruited bone cells at primary ossification centers. After adult bone fracture, dete

Gene Functions References

Overexpression of Dlx2 enhances early chondrocyte differentiation by increasing accumulation of Col2alpha1, type II collagen and aggrecan, but interferes later stages of chondrocyte differentiation through inhibiting MMP13 expression. PMID: 29787757
Malignant extracellular vesicles carrying MMP1 mRNA facilitate peritoneal dissemination in ovarian cancer. PMID: 28262727
Estrogen-related receptor gamma (ERRgamma) overexpression in chondrocytes directly upregulates matrix metalloproteinase (MMP)-3 and MMP13, which are known to play crucial roles in cartilage destruction in osteoarthritis (OA). PMID: 29247173
MMP-2 promoted and MMP-13 disrupted vasculogenic mimicry formation in large cell lung cancer by cleaving laminin-5 to influence EGFR signal activation. PMID: 28766880
The data demonstrate that MMP13 and CTGF play a crucial role in modulation of fibrogenic mediators while promoting hepatic fibrogenesis. PMID: 28782260
CXCL10 has strong inhibitory effects on neovascularization, whereas MMP13 is required for neovascularization in C. albicans-infected corneas. PMID: 28623423
that MMP-13 is a central protease in infarct development and cortical remodeling during post-stroke neurorepair PMID: 27001146
the phenotype seen in the Hdac4(-/-) mice is partially derived from elevation in MMP-13 and may be due to a bone remodeling disorder caused by overexpression of this enzyme. PMID: 27320207
data reveal a novel involvement of MMP-13 in regulating dendritic cell (DC) immunobiology through moderating MHC-I surface presentation, endocytosis and cytokine/chemokine secretion; furthermore, the reduced MHC-I surface presentation by DCs resulted in a poor CD8(+) T-cell response in vitro; MMP-13 might be a promising target for therapeutic intervention in inflammatory diseases PMID: 26921214
The progressive process of articular cartilage degeneration was significantly delayed in the knee joints of Ddr2-deficient mice in comparison to their control littermates. Articular cartilage damage in the knee joints of the mice was associated with increased expression profiles of both Ddr2 and matrix metalloproteinase 13. PMID: 27640147
Postnatal chondrocyte-specific deletion of Hdac3 with an inducible Col2a1-Cre caused premature production of pErk1/2 and Mmp13 in the growth plate. PMID: 27662443
Mmp13 is selectively regulated of by 1,25-Dihydroxyvitamin D3, PTH, and Osterix through distal enhancers. PMID: 26348136
Our study contributes to the understanding of the role of HIF1alpha in OA and highlights the HIF1alpha-beta-catenin interaction, thus providing new insights into the impact of hypoxia in articular cartilage. PMID: 27122313
Matrix metalloproteinases (MMP) are effectors of hippocampal neuroplasticity in the adult central nervous system and that the MMP-1/protease-activated receptor-1 axis may play a role in neurogenesis following physiological and/or pathological stimuli. PMID: 26783471
We reveal a novel role of AP-2epsilon in the regulation of gene expression in articular chondrocytes, as well as in osteoarthritis development, through modulation of Mmp13 expression and activity. PMID: 25964075
B-16 melanoma cells with up-regulated MMP-13 expression promoted invasion of tumor cells through Matrigel compared with control cells transfected with empty vector. Knocked-down MMP-13 expression also decreased invading cell numbers. PMID: 25749207
Data indicate that tamoxifen decreased collage type II COL2A1 by activating matrix metallopeptidases MMP-2/13 expression. PMID: 25703139
This study demonstrates that stromal as well as tumor derived MMP13 contribute to tumor cell extravasation and establishment of metastases in the liver microenvironment. PMID: 25880591
Elevated MMP13 activity may contribute to Pseudomonas aeruginosa keratitis through basement membrane degradation. PMID: 25589337
Mmp13 gene is regulated via at least three specific distal enhancers that display independent activities yet are able to integrate response from multiple signaling pathways in a model of activation and suppression. PMID: 25773540
SIRT1 activation inhibits PTH stimulation of Mmp13 expression, and this regulation is mediated by SIRT1 association with c-Jun at the AP-1 site of the Mmp13 promoter. PMID: 25631045
Mmp13 is critical for Osteoarthritis progression PMID: 23298463
the concomitant inhibition of MMP-9 and MMP-13 altered the immunogenic properties of melanoma, stimulated the lymphocytic infiltration of tumor nodules, and decreased the expression of oncomicroRNA miR-21 and miR-let-7b. PMID: 25868368
there is a strong link between lower estrogen levels in old female mice, an elevated MMP-13 level, which results in a more effective MMP-13 inhibitor treatment in fibroblasts and SCC cells in vitro and in vivo PMID: 24676718
MMP-13 deficiency acts to suppress the local inflammatory responses. Therefore, MMP-13 has a role in the pathogenesis of arthritis PMID: 24369907
Knee loading reduces MMP13 activity and suppresses cartilage destruction. PMID: 24180431
MMP-13 prevails over MMP-8 in collagen degradation in atheromata. PMID: 24723558
Stromal matrix metalloprotease-13 knockout alters Collagen I structure at the tumor-host interface and increases lung metastasis of C57BL/6 syngeneic E0771 mammary tumor cells. PMID: 24010522
ANKRD1, in association with factors such as nucleolin, represses MMP13 transcription. Ankrd1 deletion additionally relieved MMP10 transcriptional repression PMID: 24515436
Relaxin and estrogen caused greater induction of MMP13 vs. MMP9 in temporomandibular joint. PMID: 24640575
presence of MMP-13 seems to limit the overall extent of ECM deposition in lung fibrosis PMID: 24023851
epithelial expression of MMP-1 inhibits mitochondrial function, increases HIF-1alpha expression, decreases reactive oxygen species production, and contributes to a proliferative, migratory, and anti-apoptotic AEC phenotype. PMID: 23902766
Mmp13-dependent intestinal Tumor Necrosis Factor activation results in mucus depletion, increased intestinal inflammation, systemic inflammation and organ damage. PMID: 23723167
MMP-13 has a primary role in myoblast migration that leads to secondary effects on differentiation, and is a new contributor to skeletal muscle regeneration. PMID: 23761625
Noncanonical MMP-1-PAR1 signaling resulted in the opposite effect and led to a dedifferentiated phenotype via a different G protein pathway. MMP-1-PAR1 significantly stimulated hyperplasia and migration of SMCs. PMID: 23814055
GPR64 expression in ES maintains an immature phenotype that is less sensitive to TRAIL-induced apoptosis and via its up-regulation of PGF and MMP1 orchestrates and promotes invasiveness and metastatic spread in Ewing sarcoma. PMID: 23338946
Matrix metalloproteinase 13 (MMP13) is a direct target of osteoblast-specific transcription factor osterix (Osx) in osteoblasts. PMID: 23185634
regulation of a11b1-dependent matrix remodeling, involving MMP-13 , might also occur in other types of fibroblasts and be an important regulatory mechanism for coordinated extracellular and intracellular collagen turnover in tissue homeostasis PMID: 23065814
The findings of the present study reveal an important role of MMP-1 in OS primary tumor and metastasis formation to the lung, the major organ of osteosarcoma metastasis. PMID: 23195950
microRNA miR-199a-5p down-regulation switches on wound angiogenesis by derepressing the v-ets erythroblastosis virus E26 oncogene homolog 1-matrix metalloproteinase-1 pathway PMID: 23060436
Suture compression elevated the MMP-1 and 13 expressions, activated osteoclasts, reduced bone density, and induced bone resorption adjacent to the suture. It suggests that suture compression can be used for bone volume reduction PMID: 22819631
These results provide evidence for an important role for MMP-13 in wound healing by coordinating cellular activities important in the growth and maturation of granulation tissue. PMID: 22880047
Osteocyte perilacunar remodeling of mid-cortical bone matrix requires MMP-13 and is essential for the maintenance of bone quality. PMID: 22549931
Osterix regulates calcification and degradation of chondrogenic matrices through matrix metalloproteinase 13 (MMP13) expression in association with transcription factor Runx2 during endochondral ossification PMID: 22869368
demonstrate that beta-adrenergic receptor stimulation leads to MMP-13 transactivation of protease-activated receptor 1 in both cardiac fibroblasts and cardiomyocytes PMID: 22610965
MMP-1, -3 and -9 genes are upregulated by West Nile virus infection in the blood-brain barrier. PMID: 22398316
findings show that C/EBPbeta and RUNX2, with MMP-13 as the target and HIF-2alpha as the inducer, control cartilage degradation PMID: 22095691
certain proteases, such as Mmp1, play a pivotal role in certain proteases, such as MT1-MMP, play a pivotal role in PO-induced matrix remodeling and fibrosis-induced matrix remodeling and fibrosis PMID: 22287584
a novel role for ELF3 as a procatabolic factor that may contribute to cartilage remodeling and degradation by regulating MMP13 gene transcription. PMID: 22158614
Wnt5a-Ror2 signaling might also be required for expression of MMP-13 gene during the development of the cartilaginous tissue. PMID: 22128168

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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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