Recombinant Human Collagenase 3 (MMP13) Protein (His-SUMO)

Name: Recombinant Human Collagenase 3 (MMP13) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03106P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Collagenase 3 (MMP13) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P45452
Target Symbol	MMP13
Synonyms	CLG 3; CLG3; Collagenase 3; Collagenase3; MANDP1; Matrix metallopeptidase 13 (collagenase 3); Matrix Metalloproteinase 13; Matrix metalloproteinase-13; MMP 13; MMP-13; Mmp13; MMP13_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC
Expression Range	104-471aa
Protein Length	Full Length of Mature Protein
Mol. Weight	58.3kDa
Research Area	Developmental Biology
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	HGNC: 7159 OMIM: 250400 KEGG: hsa:4322 STRING: 9606.ENSP00000260302 UniGene: PMID: 29345283 Data suggest that matrix metalloproteinase 13 (MMP-13) and its regulatory networks are suitable targets for the development of effective early treatment strategies for osteoarthritis (OA). PMID: 29126436 High Expressions of MMP-13 is associated with degenerative knee osteoarthritis. PMID: 28418842 Transfection of cells with either miR-100 or miR-125b negated the induction of MMP13 release. Additionally, AR activation induced a morphological alteration of MDA-MB-453 cells, which was blocked by miR-125b only. PMID: 28816390 ATM could be activated by lung cancer-associated TNF-alpha, up-regulate MMP-13 expression and thereby augment tumor metastasis PMID: 27556690 The Sp1-mediaded allelic regulation of MMP13 expression by an esophageal squamous cell carcinoma susceptibility SNP rs2252070 has been demonstrated. PMID: 27245877 MMP-13 IRS represents a suitable method to assess pathologic grade of precancerous and cancerous colorectal lesions. MMP-13 has been identified as an excellent marker of high grade IEN and CRC, and may thus be applied for prognostic stratification. PMID: 27716617 These findings suggest that using MMP-13 inhibitors in diffuse group might contribute to the control of tumor growth PMID: 28128735 A strong association between the -77 MMP-13 polymorphism and posterior tibial tendinopathy insufficiency. PMID: 27886420 TGF-beta1 stimulates the phosphorylation of Runx2 at three serine amino acids, and this event is required for MMP-13 expression in osteoblastic cells. PMID: 28419442 IL-6-stimulated MMP-13 expression was independent of IL-1beta stimulation and was blocked by SAHA, suggesting that SAHA inhibits IL-6 signaling in Osteoarthritis (OA) chondrocytes. PMID: 27555113 High MMP13 expression is associated with intervertebral disc degeneration. PMID: 28559201 data demonstrate that MMP-13 is critical for the development of osteolytic lesions in Multiple myeloma and that targeting the MMP-13 protein - rather than its catalytic activity - constitutes a potential approach to mitigating bone disease in affected patients. PMID: 27043283 Endoplasmic reticulum stress participates in the progress of senescence and apoptosis of osteoarthritic chondrocytes, which manifested in increased expression of ADAMTS5, MMP13, and decreased COL2A1 expression. PMID: 28728848 these findings support roles for both cFOS (indirect) and ATF3 (direct) in effecting MMP13 transcription in human chondrocytes. PMID: 27956552 In osteoarthritis (OA) chondrocytes, hydrostatic pressure (HP) restores the expression levels of some miRNAs, downregulates MMP-13, ADAMTS-5, and HDAC-4, and modulates the Wnt/beta-catenin pathway activation. PMID: 28085114 These results suggested that HIF-2alpha may cause meniscal matrix degradation by transactivation of MMP-13 PMID: 26892680 TGF-beta1 stimulated a sustained and prolonged expression of ATF-3, and its interaction and regulation of c-Jun protein and their assembly as a protein complex at the AP-1 site of the MMP-13 promoter could be responsible for MMP-13 gene activation in MDA-MB231 cells. PMID: 27751807 Serum MMP13 did not differ significantly between normal weight, overweight, and obese participants. PMID: 27296149 No significant association was observed in MMP13, TIMP2 and TGFB3 genes with CP or PI. CP is a risk factor to develop PI, however, there is no association of both diseases with polymorphisms in the MMP13, TIMP2 and TGFB3 genes PMID: 27058373 Findings suggest thatSirt1 may regulate the expression of Runx2, which is the osteogenic transcription factor, and the production of MMP-13 from chondrocytes in OA. PMID: 27367673 the mechanisms and roles of MMP-13 secretion in human small airway epithelial cells and functional polymorphisms of the MMP13 gene PMID: 26635116 as the grade of late-stage osteoarthritis advanced, levels of TNF-alpha in the serum became elevated, whereas levels of MMP-13 in the synovial fluid became elevated PMID: 27130394 As the grade of late stage osteoarthritis advances, increase in synovial MMP-13 and serum TNF-a levels become pronounced. PMID: 27932045 High MMP13 serum levels are associated with Esophageal Squamous Cell Carcinoma. PMID: 27356690 Our study demonstrates that miR-148a inhibits the migration of breast cancer cells by targeting MMP-13 PMID: 26298724 MMP13 expression positively related to the lymph node and distal metastasis, tumor stage and relapse of colorectal cancer PMID: 25726157 in degenerative intervertebral discs, IL1b upregulates NFkB, MMP13 and ADAMTS4 PMID: 25433723 Expression of MMP13 negatively correlated with miR-27b expression in degenerative nucleus pulposus tissues. PMID: 26583473 sustained released resveratrol inhibits interleukin-1beta-induced metalloproteinase-13 activation and promotes chondrocyte differentiation PMID: 26526931 Report modified platelet deposition on matrix metalloproteinase 13 digested collagen I PMID: 26447617 GP73 enhances MMP-13 expression through cAMP responsive element binding protein (CREB)-mediated transcription activation. Levels of GP73 and MMP-13 are increased and positively correlated in human HCC tissues. Augmented MMP-13 potentiates HCC cell metastasis. PMID: 26378022 SENP2 inhibits MMP13 expression in BC cells through de-SUMOylation of TBL1/TBLR1, which inhibits nuclear translocation of beta-catenin. PMID: 26369384 Hyaluronic acid exhibits a pronounced suppressive effect on MMP-13 expression in osteoarthritis. PMID: 26934732 Elevated levels of MMP-13 may play a role in the pathogenesis of chronic periodontitis. There is a direct correlation of increased expression of MMP-13 with various clinical and histologic parameters in disease severity PMID: 25006778 IL-1Ra is associated with MMP-13 expression and has a novel function in such regulation without interference of the IL-1 signaling cascade. PMID: 26474296 siRNA inhibited the effect of MMP13-containing exosomes on tumor cells metastasis as well as angiogenesis PMID: 26362844 RKIP Inhibits Local Breast Cancer Invasion by Antagonizing the Transcriptional Activation of MMP13 PMID: 26308852 together, these data demonstrate that SERPINE2 might prevent cartilage catabolism by inhibiting the expression of MMP-13, one of the most relevant collagenases, involved in cartilage breakdown in OA. PMID: 26305372 High expression of matrix metalloproteinase-13 is associated with pancreatic cancer. PMID: 25948792 Together, these data suggest that shikonin may suppress Osteosarcoma invasiveness through MMP13 suppression. Thus, our data highlight a previous unappreciated role for shikonin in suppressing Osteosarcoma cell metastasis PMID: 26104765 our results revealed that activation of the P2X7 receptor by ATP promotes breast cancer cell invasion and migration, possibly via activation of the AKT pathway and regulation of E-cadherin and MMP-13 expression. PMID: 25976617 MMP-13 was associated with metastasis and poor survival in 79 patients with melanoma. MMP-13 expression was inversely correlated with vasculogenic mimicry. MMP-13 cleaves laminin-5 gamma 2 to accelerate metastasis. PMID: 25749207 Together, these data suggest that GRh2 may suppress GBM migration through inhibiting Akt-mediated MMP13 activation. PMID: 25835975 Both VEGF-C and MMP13 are significantly upregulated in Multiple Myeloma with lymph-node metastases. PMID: 25966777 IL-32 stimulation promotes the invasion and motility of osteosarcoma cells, possibly via the activation of AKT and the upregulation of MMP-13 expression. PMID: 25846944 Up-regulation of matrix metalloproteinase 13 is associated with colitis-associated cancer. PMID: 25742789 Data show that knockdown of endogenous periostin attenuates constitutive matrix metalloproteinase-13 (MMP-13) expression. PMID: 26092928 Clusterin is an independent predictive factor for prognosis of hepatocellular carcinoma and it facilitates metastasis through EIF3I/Akt/MMP13 signaling. PMID: 25609201 High level of protein expression of MMP13 was significantly associated with poor prognosis in oral squamous cell carcinoma. PMID: 25401159

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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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