Code | CSB-EP014660MO |
Size | US$2466 |
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Description |
The process of expressing this Mouse Mmp13 recombinant protein in E.coli expression system requires the following steps: use of competent E. coli cells to take up DNA sequence of interest, the exogenous plasmid is transferred into the cell, and the transcription and translation are directly replicated in the cell, selection of transformed E. coli using a selection marker, expansion of selected E. coli to a higher scale in appropriate culture media, such as classic LB options Growth Systems and lastly isolation and purification.And we finally get a Mmp13 protein with N-terminal 6xHis tag and it is determined by SDS-PAGE with a purity of 90%+. MMP13 is a protein coding gene that encodes Collagenase 3 (Matrix metalloproteinase-13). According to some studies, MMP13 may have the following features.MMP13 is a key target gene in the progression of osteoarthritis. MiR-9 was found to inhibit the secretion of type II collagen-targeted metalloproteinase MMP13 in isolated human chondrocytes. MMP13 may be a new tumor marker for the diagnosis of breast cancer. MMP13 is a stromal mediator that controls persistent angiogenesis in skin cancer. circRNA-CER participates in chondrocyte ECM degradation by regulating the expression of MMP13 as a competing endogenous RNA. MMP13 polymorphism reduces the risk of dental caries. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Target Names | Mmp13 |
Uniprot No. | P33435 |
Research Area | Others |
Alternative Names |
Mmp13; Collagenase 3; EC 3.4.24.-; Matrix metalloproteinase-13; MMP-13
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Species | Mus musculus (Mouse) |
Source | E.coli |
Expression Region | 105-472aa |
Target Protein Sequence | YNVFPRTLKWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSILWC Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
Mol. Weight | 46.5kDa |
Protein Length | Full Length of Mature Protein |
Tag Info |
N-terminal 6xHis-tagged |
Form |
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. |
Buffer | 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. |
Reconstitution | 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 |
Protein 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 |
Notes | 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. |
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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.
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Gene References into Functions |
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Subcellular Location | Secreted, extracellular space, extracellular matrix. Secreted. |
Protein Families | Peptidase M10A family |
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 |
Database Links |
KEGG: mmu:17386 STRING: 10090.ENSMUSP00000015394 UniGene: Mm.5022 |