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Validated All-in-One™ qPCR Primer for MMP12(NM_002426.5) Search again
Product ID:
HQP011266
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HME, ME, MME, MMP-12
Gene Description:
matrix metallopeptidase 12
Target Gene Accession:
NM_002426.5(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq].
Gene References into function
- substrate specificity based on x ray crystallography
- crystal structure in complex with hydroxamic acid inhibitor
- These data suggest that polymorphisms in the MMP1 and MMP12 genes, but not MMP9, are either causative factors in smoking-related lung injury or are in linkage disequilibrium with causative polymorphisms.
- The presence of MMP-12 has been demonstrated in multiple sclerosis (MS) lesions, particularly in foamy macrophages in actively demyelinating lesions, suggesting a role for MMP-12 during demyelination in MS.
- Migration of monocytes/macrophages in vitro and in vivo is accompanied by MMP12-dependent tunnel formation and by neovascularization.
- MMP-12 is expressed in and secreted by human bronchial epithelial cells
- abnormal production of tropoelastin and fibrillin by heat in human skin and that their degradation by various MMP, such as MMP-12, may contribute to the accumulation of elastotic material in photoaged skin.
- MMP-12 might be not only a prognostic marker, but also a valuable therapeutic target.
- Chronic obstructive pulmonary disease patients produce greater quantities of MMP-12 than controls
- findings provide novel evidence of a direct relationship between cigarette smoke exposure and MMP-12 in human airway epithelia and suggest several targets for modulation of this potentially pathogenic pathway
- By regulating the proliferation of corneal epithelial cells, Wnt-7a and MMP-12 appear to contribute to corneal wound healing
- NADPH oxidase restrains the MMP-12 activity of macrophages
- cathepsin F, matrix metalloproteinases 11 and 12 are upregulated in cervical cancer
- Matrix metalloproteinase 12, a proteinase that plays a critical role in mouse models, was the third most highly induced gene in smokers (ninefold, p < 0.0001).
- matrix metalloproteinase 1, 3 and 12 haplotypes may associated with development of lung cancer, particularly among never smokers and men
- Our findings indicate that human airway smooth muscle cells express and secrete MMP-12 that is up-regulated by IL-1beta and TNF-alpha.
- analysis of substrate specificity of matrix metalloproteinase-12
- Protective role for stromal MMP-12 in lung tumor growth; the use of the human/mouse protein chips allows us to distinguish tumor and host-derived proteases
- A new factor, MMP-12, regulates glioma invasiveness through interaction with tenascin-C.
- NMR structure of matrix metalloproteinase 12
- MMP-12 is an important oncogene in high-stage and high-grade endometrial adenocarcinoma.
- Reliable and reproducible estimates of k(cat)and K(m) from only two or three progress curves were obtained using MMP12.
- Results describe copy number aberrations in the SDHD and MMP12 genes in an affected Solar Keratosis and control cohort.
- Inhibitor-binding-induced perturbations of the NMR spectra of MMP-1 and MMP-3 map to similar locations across MMP-12 and encompass the internal conformational adjustments
- Smoking and disease itself may stimulate MMP-12 expression in airway compartments (sputum and bronchoalveolar lavage)from chronic obstructive pulmonary disease patients.
- results indicate that resident alveolar macrophages and recruited neutrophils do not play a role in the delayed macrophage recruitment induced by rhMMP-12
- 357Asn/Ser polymorphism not related to generalized aggressive periodontitis
- data suggest that MMP-2 -735C/T, MMP-9 -1562C/T and MMP-12 357Asn/Ser polymorphisms are not associated with susceptibility to severe CP in Turkish population. T allele of MMP-9 -1562 gene might be associated with decreased susceptibility to severe CP.
- Alveolar macrophage matrix metalloproteinase 1 and 12 may have a role in the lung structural changes leading to the development of emphysema.
- potential role for MMP12 -82 A/G and MMP13 -77 A/G combined polymorphisms in superficial endometriosis. As no association was found with deep infiltrating endometriosis, these polymorphisms might protect from a more in-depth penetration of tissues.
- Bone Marrow Stromal (BMS) cells induce MMP-12 expression in prostate cancer cells, which results in invasive cells capable of degradation of type I collagen.
- The amino acid preferences of the different subsites on the catalytic domain of MMP-12 were analyzed.
- we conclude that one mechanism, by which MMP-12 induces IL-8/CXCL8 release from the alveolar epithelium, is the EGFR/ERK1/2/activating protein-1 pathway.
- MMP-12 may be critical to the initiation and progression of atherosclerosis via degradation of the elastic layers and/or basement membrane.
- NMR-derived structure of catalytic domain of MMP12 is complex with N-(dibenzo[b,d] thiophene-3-sulfonyl valine.
- MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity
- MMP-12 truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists
- Molecular determinants of matrix metalloproteinase-12 covalent modification by a photoaffinity probe: insights into activity-based probe development and conformational variability of matrix metalloproteinases
- Our results show that MMP-12 expression (mRNA and protein) is down regulated in IL-1beta-treated macrophages only in the presence of a specific PPARalpha agonist, GW647, in a dose-dependent manner.
- MMP-12 were identified at higher levels in lung secretions of pediatric ALI patients compared with controls.