Recombinant Human Macrophage Metalloelastase (MMP12) Protein (His)

Name: Recombinant Human Macrophage Metalloelastase (MMP12) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02363P
Price: 418.4 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 Homo sapiens (Human) MMP12.

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

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Product Overview

Description	Recombinant Human Macrophage Metalloelastase (MMP12) 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	P39900
Target Symbol	MMP12
Synonyms	EC 3.4.24.65; HME; Macrophage elastase; Macrophage metalloelastase; Macrophage metaloelastase; Matrix metallopeptidase 12 (macrophage elastase); Matrix metalloprotease 12; Matrix metalloproteinase-12; ME; MGC138506; MME; MMP 12; MMP-12; Mmp12; MMP12_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC
Expression Range	106-470aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.1kDa
Research Area	Cancer
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	May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Peptidase M10A family
Database References	HGNC: 7158 OMIM: 601046 KEGG: hsa:4321 UniGene: Hs.1695
Tissue Specificity	Found in alveolar macrophages but not in peripheral blood monocytes.

Gene Functions References

Studied association of matrix metallopeptidase 12 (MMP12) -82 A>G promoter single nucleotide polymorphism (SNP) with bronchial asthma in a Bulgarian population. Results suggest the variant G allele of the MMP12 -82 A>G promoter polymorphism might considered protective for development of bronchial asthma. PMID: 29390099
that MMP-12 might act as a potential target for the development of novel therapeutics of esophageal squamous cell carcinoma PMID: 29033183
MMP-12 (-82A/G) polymorphisms associate with obesity risk and its severity. PMID: 29317790
Significant association observed for MMP-12 (-1082 A/G) (OR 2.55; 95% CI 1.75 to 3.71) gene polymorphism and risk of ischemic stroke. [meta-analysis] PMID: 29906531
The MMP12 down regulation by increasing oxygen concentration enables temporal expression control of MMP12 and involves several mechanisms including HIF-1alpha. These findings suggest MMP12 involved in trophoblast invasion during the first trimester. PMID: 28990117
In the present report, hypoxia is shown to activate a HIF-KDM3A-MMP12 signaling cascade that promotes trophoblast invasion and trophoblast-directed uterine spiral artery remodeling. PMID: 27807143
The current results suggest that MMP12 rs652438 but not MMP12 rs2276109 may affect the risk for Parkinson Disease PMID: 28655442
M4 macrophages are a possible source for HDAC9 and MMP12 expression in advanced human carotid plaques. PMID: 28343758
MMP12 levels were increased in gingival tissue of periodontitis patients. MMP12-producing monocyte-derived cells also had reduced CD200R surface levels. MMP12 production by these cells was induced by CSF2, and treatment with a CD200R ligand reduced CSF2-induced MMP12 production. This novel association of the CD200/CD200R pathway with MMP12 production by monocyte-derived cells may play a key role in PD progression. PMID: 29101312
G allele of MMP12 -82 A > G promoter polymorphism as a protective factor for COPD in Bulgarian population PMID: 28692348
We also found that MMP12 facilitated type I collagen induced platelet aggregation, adhesion and alpha granule secretion. Similarly, one short peptide, WYKG, facilitated type I collagen induced platelet alpha granule secretion. We conclude that platelet express MMP12 may facilitate platelet activation through shedding of CEACAM1. PMID: 28385529
To conclude, Pseudomonas aeruginosa infection induced the expression of matrix metalloproteinases, and Pseudomonas aeruginosa type III secretion system appeared to be a key player in MMP-12 and MMP-13 expression, which is further controlled by NF-kappaB signaling. PMID: 27377745
This study demonstrated that the MMP-12 levels was significantly higher in patients with atheromatous plaques than in those without plaques. PMID: 27345464
High MMP12 expression is associated with gastric cancer. PMID: 28098914
Study evaluated MMP-12 and TIMP-1, TIMP-2, TIMP-3, and TIMP-4 levels in 40 patients with asymptomatic and symptomatic critical carotid artery stenosis (CAS) with neurologic symptoms onset within the preceding 12 hours; results suggest that MMP-12 is related to critical CAS independently on symptoms, moreover, TIMP-3 and TIMP-4 seem to be specifically related to stroke PMID: 27746079
MMP12 causes arterial stiffening in mice and suggest that it functions similarly in humans. PMID: 26608672
Productive complex between MMP-12 and synthetic triple-helical collagen V, are revealed through paramagnetic NMR. PMID: 26887942
These results proved that MMP-12 expression was increased in cutaneous melanoma and associated with tumor progression. It also provided the first evidence that MMP-12 level could be an independent prognostic marker for patients with cutaneous melanoma PMID: 26040769
fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF) B and D, which in turn transactivate MMP-12. PMID: 25435370
AG and GG genotypes of the MMP12 rs2276109 variant were significantly under-represented among patients with non-contact anterior cruciate ligament rupture compared to controls. PMID: 21410539
HnRNP K can induce MMP12 expression and enzyme activity through activating MMP12 promoter, which promotes cell migration and invasion in nasopharyngeal carcinoma cells. PMID: 24885469
We identified a novel association with an MMP12 locus in large artery atherosclerosis (rs660599; p = 2.5x10), with independent replication in a second population PMID: 25078452
Thrombin-activated microglia expression of tumor necrosis factor-a, interleukin-1b and MMP-12 was significantly reduced through contact-dependent and paracrine mechanisms when the HAESCs were co-cultured with microglia cells PMID: 24424266
Macrophage MMP12 regulates adipose tissue expansion, insulin sensitivity, and expression of inducible nitric oxide synthase. PMID: 24914938
MMP12 is located in genes previously associated with chronic obstructive pulmonary disease susceptibility. PMID: 25006744
In acute aortic dissection patients, macrophage activation is strongly related to the clinical outcome of atherosclerotic disease and the role of MMP-12 as a specific marker. PMID: 24432723
In emphysema, MMP12 mRNA expression was inversely related to the diffusing capacity of the lung. PMID: 23900981
These findings suggest that inhibiting extracellular MMP-12 could be a new avenue for the development of antiviral treatments PMID: 24784232
role of matrix metalloproteinase 12 in non-small cell lung cancer PMID: 24398311
MMP-12 proteolytic activity exists within the aorta specimens and blood samples from aortic dissection patients. PMID: 23642232
The present study evaluated the association between these single nucleotide polymorphisms in MMP12 and MMp13 in patients with colorectal cancer (CRC) patients and healthy controls. PMID: 23898086
MMP-12 expression was found to be significantly associated with extracapsular spread and correlated with nodal metastasis in head and neck squamous cell carcinoma. No relation was found between MMP expression and survival. PMID: 22907031
the endogenous matrix metalloprotease-12 active form can be detected with a novel broad spectrum activity-based probe PMID: 23271741
confers susceptibility to asthma and is associated with asthma severity in a Japanese population PMID: 23075521
Suggest that the inter-individual variability in the MMP-12 gene variation may not be a risk factor for vulnerable plaques in the Chinese Han population. PMID: 22863605
Studied the catalytic domain of MMP-12 in complex with the known inhibitor CGS27023A. A 3D (15)N-edited/(14)N,(12)C-filtered ROESY experiment was used to monitor and distinguish protein amide protons in fast exchange with bulk water. PMID: 22528292
Our results establish microglia as a significant source of progranulin(PGRN), and MMP-12 as modulators of PGRN PMID: 22509390
analysis of orally potent and selective small molecule inhibitor of MMP-12 for treatment of COPD and asthma in human and mouse models PMID: 22153340
Sputum MMP-12 concentrations and activity in patients with chronic obstructive pulmonary disease are associated with the extent of emphysema PMID: 22305682
MMP-12 participates in experimental small airway modelling and in emphysema [review] PMID: 21920892
Provide in vivo evidence of an effect of MMP12 on fibrinogen level. PMID: 22119538
Surfaces of MMP-12 far from its active site have been found to affect degradation and affinity for elastin substrates; main exosite 1 has been extended to Asp-124 that binds calcium while exosite 2 comprises residues near the back of the catalytic domain. PMID: 21967233
rs652438 SNP alters MMP-12 activity with the A allele being more active, which is associated with increased macrophage infiltration and emphysema in the lungs of patients with COPD. These findings further implicate MMP-12 and this SNP in COPD PMID: 21730350
MMP-12 mRNA may be a valuable prognostic marker for both overall survival and tumour recurrence of hepatocellular patients after liver resection. PMID: 21683576
High expression of MMP-12 in squamous laryngeal carcinoma was related to significant hyperplasia. PMID: 17357518
Data suggest that the matrix metalloproteinase-12 rs2276109 gene polymorphism may contribute to susceptibility to systemic sclerosis (SSc), and in particular to diffuse cutaneous SSc and pulmonary fibrosis. PMID: 20595276
Overexpression of human macrophage metalloelastase is strongly correlated with the reduced angiogenesis and vascular invasion of gastric carcinoma, and may serve as a useful predictive indicator in patients with this disease. PMID: 20127415
distribution of N357S genotypes not significantly different in chronic obstructive pulmonary disease PMID: 20160424
Individuals with MMP-12 -82A/G and MMP-13 -77A/A might have higher risk of overall or special histological type of epithelial ovarian carcinoma development. PMID: 20376807
The catalytic domain of MMP-12 binds to the triple helix and cleaves the typical sites -Gly(775)-Leu(776)- in alpha-2 type I collagen and -Gly(775)-Ile(776)- in alpha-1 type I and type III collagens and at multiple other sites in both collagen types. PMID: 19932771

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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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