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Validated All-in-One™ qPCR Primer for MMP8(NM_002424.2) Search again
Product ID:
HQP011262
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CLG1, HNC, MMP-8, PMNL-CL
Gene Description:
matrix metallopeptidase 8
Target Gene Accession:
NM_002424.2(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. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq].
Gene References into function
- expression in normal and malignant melanocytic cells
- MMP-8 cleaves TFPI following Ser(174) within the connecting region between the second and third Kunitz domains
- gelatinase B and neutrophil collagenase cleave MIG and IP-10
- Matrix metalloproteinase-8 is produced primarily by chorionic cells in human fetal membranes, and the level of matrix metalloproteinase-8 protein and messenger RNA expression in fetal membranes increases during labor.
- membrane-bound MMP-8 on PMN cleaves types I and II collagens, and alpha(1)-proteinase inhibitor, but is substantially resistant to inhibition by tissue inhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2.
- Functionally significant single nucleotide polymorphisms of the MMP8 promoter haplotypes and preterm premature rupture of membranes were evaluated.
- in the later stages of myeloid development, MMP8 and other SGP genes are coordinately upregulated, and members of the C/EBP family, in particular C/EBPalpha and C/EBPepsilon, play specific and unique roles in upregulating their expression
- Significantly elevated metalloproteinase 8 in broncho-alveolar lavage fluid is associated with Bronchiolitis obliterans
- significantly elevated sinus mucus levels associated with elevated IL-8 levels in chronic rhinosinusitis with nasal polyposis (CRSwNP); IL-8 and MMP-8 seemingly form an inductive cytokine-proteinase cascade in CRSwNP pathogenesis
- x-ray crystallographic analysis reveals that in a complex with MMP-8, N-hydroxyurea binds the catalytic zinc ion in a monodentate rather than bidentate mode and with high out-of-plane distortion of the amide bonds
- MMP-8 has a role in carotid plaque progression
- A localized increase in MMP-8 and -9, mediated by native mesenchymal cells, presents a potential pathway for collagen breakdown and abdominal aortic aneurysm rupture.
- findings show that bacterial vaginosis is associated with increased levels of matrix metalloproteinase-8(MMP-8) in vaginal fluid
- The expression of matrix-modeling genes in chronic idiopathic myelofibrosis (cIMF) is not influenced by the JAK2 mutation status but is predominantly related to the stage of disease.
- Immunofluorescence intensity, representing MMP-8 expression, in the periodontal tissues of smokers (30 fields from 6 subjects, mean 1154+/-124 units) was significantly higher than that in the periodontal tissues of non-smokers.
- distinct deficits in NO production and elevations in MMP-8 and -9 expression in diabetic human skin fibroblasts compared to normal
- C-terminus of ephrin-B1 regulates activation of the extracellular release of MMP-8 without requirement of de novo protein synthesis.
- Results show that -799C/T on the promoter region of MMP-8 lacks association with development of bronchiectasis in Koreans.
- Serum MMP-8 concentrations are elevated in prevalent or subclinical atherosclerosis and associate with the worst cardiovascular outcome.
- MMP8 gene variation may influence breast cancer prognosis and support the notion that MMP8 has an inhibitory effect on cancer metastasis.
- In an in vitro atherosclerosis model neutrophil infiltration was mediated via IL-8-signalling and accompanied by release of MMP-8 and induction of endothelial cell apoptosis.
- MMP8, but not MMP1 or MMP13, may affect the metastatic behaviour of breast cancer cells through protection against lymph node metastasis
- Total MMP-8 immunoreactivity, the proportion of active MMP-9, and gelatinolytic activity in urine were significantly higher in diabetic nephropathy patients than in controls
- high serum MMP-8 levels in melanoma patients were significantly related to presence of vascular invasion (P=0.001) in primary tumour, tumour ulceration (P=0.003) and tumour bleeding (P=0.033)
- In patients with high-risk bacteria, MMP-8-, MMP-9- and TIMP-1-concentrations were higher than in patients with low-risk bacteria.
- Functional polymorphisms in the promoter of MMP-8 do not significantly confer susceptibility to hepatocellular carcinoma in a southern Chinese population.
- Non-surgical periodontal treatment was effective in reducing the levels of MMP8 in gingival crevicular fluid from diabetic patients with chronic periodontitis.
- a C/G polymorphism in MMP8 was associated with a statistically significant decreased risk of developing lung cancer, but does not seem to modify or be an independent prognostic factor for overall survival
- MMP-8 were identified at higher levels in lung secretions of pediatric ALI patients compared with controls.