Analytical Data
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Gene name
MMP12
- Application
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Alternative Names
MMP12；HME；Macrophage metalloelastase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P39900
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Expression Region
1-470aa
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AA Sequence
MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPV TKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHF REMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFS KINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDED EFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRL SADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFF FKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDD KYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQY WRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFE YDFLLQRITKTLKSNSWFGC
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Molecular Weight
80 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Matrix metalloproteinase-12 (MMP12), also known as macrophage metalloelastase, is an important enzyme involved in the degradation of extracellular matrix components, playing a crucial role in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammation. Its specificity for elastin and other extracellular matrix substrates links it to several diseases, particularly those characterized by excessive tissue remodeling such as chronic obstructive pulmonary disease (COPD), atherosclerosis, and cancer. Research on MMP12 has gained momentum due to its potential as a therapeutic target and biomarker. Its expression is primarily regulated by pro-inflammatory cytokines, making it a key player in inflammatory responses. Investigating MMP12 in the context of disease mechanisms has elucidated its contribution to the pathogenesis of chronic inflammatory diseases and tissue damage. The production of recombinant MMP12 protein facilitates detailed studies of its structure, function, and interactions with inhibitors and substrates, paving the way for the development of novel therapeutic strategies. Understanding MMP12's role at the molecular level offers insights into its involvement in disease processes and may lead to innovative approaches for modulating its activity in various clinical settings. This research contributes to the broader understanding of metalloproteinase families and their implications in health and disease.
