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Validated All-in-One™ qPCR Primer for TIMP3(NM_000362.4) Search again
Product ID:
HQP018094
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HSMRK222, K222, K222TA2, SFD
Gene Description:
TIMP metallopeptidase inhibitor 3
Target Gene Accession:
NM_000362.4(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
This gene belongs to the TIMP gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix (ECM). Expression of this gene is induced in response to mitogenic stimulation and this netrin domain-containing protein is localized to the ECM. Mutations in this gene have been associated with the autosomal dominant disorder Sorsby's fundus dystrophy. [provided by RefSeq].
Gene References into function
- Expression of Sorsby's fundus dystrophy mutations in human retinal pigment epithelial cells reduces matrix metalloproteinase inhibition and may promote angiogenesis
- Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway
- Novel mutation in TIMP3 gene causes Sorsby Fundus Dystrophy.
- Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme
- role in inducing apoptosis in retinal pigment epithelium and other cells
- TIMP-3 may contribute to the regulation of myocardial remodeling and its reduction may promote a transition from compensated to end-stage congestive heart failure.
- we demonstrate the ability of TIMP3 to inhibit vascular endothelial factor (VEGF)-mediated angiogenesis
- This protein is downregulated in lymphangioleiomyomatosis as a consequence of abnormal serum response factor expression.
- TIMP-3 promotes apoptosis in melanoma cells through stabilization of three distinct death receptors and activation of their apoptotic signaling cascade through caspase-8.
- Down-regulation of TIMP3 expression by methylation is associated with uveal melanoma development
- Peaks during the early to mid-luteal phase. Seems to play role in hormonal regulation and endometrial tissue remodeling.
- ADAM-17/TACE and TIMP-3 might play an important role in the pathogenesis of prostate cancer
- Our analysis of the entire coding region of TIMP-1, -2, and -3, which are the main inhibitors of metalloproteinase activity in the extracellular matrix, failed to show an association between genetic polymorphisms and an intracranial aneurysm
- TIMP-3 is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1)
- Reactive oxygen species mediate TGF-beta1-induced TIMP-3 gene expression
- Dermal wound healing in red Duroc pigs show unique mRNA expression of HSP47,BMP-1,TIMP1-3 and hypercontracted,hyperpigmented scars.
- Promoter methylation of the TIMP3 is involved in suppression of TIMP3 expression in choriocarcinoma.
- HBV affects the malignance of hepatocellular cancer by suppressing TIMP-3.
- role in down regulation of proMMP-2 activation in scirrhous gastric carcinoma
- Decreased expression of TIMP-3 protein correlates with invasive activity and metastasis in esophageal squamous cell carcinoma
- Activation of ERK-MAPK pathway and Sp1 transcription factor play a pivotal role in the induction of TIMP-3 by TGF-beta in chondrocytes.
- The TIMP3 modulate extracellular matrix remodeling during embryonic development and disease.
- TIMP3 inactivation occurs in the progression to secondary gliomas.
- negative effect of TGFbeta1 on ADAMTS-1, -5, -9, and -15 coupled with increases in their inhibitor, TIMP-3 may aid the accumulation of versican in the stromal compartment of the prostate in BPH and prostate cancer
- Reduced expression of TIMP-3 protein in esophageal adenocarcinoma is associated with increased tumour invasiveness
- TIMP3 seems to play an important role in the tumorigenesis of primary pancreatic adenocarcinomas
- Sequence analysis showed a single base pair change resulting in a Ser170Cys mutation in exon 5 of TIMP3
- Intracellularly produced TIMP-3 not only induces apoptosis, but also modulates the apoptosis-inhibiting effects of TNF-alpha in human rheumatoid arthritis synovial fibroblast-like cells.
- genetic variation in TIMP3 may contribute to the pathogenesis of abdominal aortic aneurysm
- TIMP-3 reactive site mutations disrupt inhibition of matrix metalloproteinases but not TACE
- Increased deposition of active TIMP-3, rather than dysregulation of metalloproteinase inhibition, is likely to be the primary, initiating event in Sorsby's fundus dystrophy .
- role in reduction of metastasis in breast cancer cell line
- Review discusses how, despite the lack of inherited mutations in the structural gene, the TIMP3 protein might play a role in the onset and progression of age-related macular degeneration.
- The inhibition of ADAMTS-2 by TIMP-3 alone out of 4 TIMP proteins is reported.
- Aberrant methylation and hence silencing of TIMP3, SLC5A8, DAPK and RARbeta2, in association with BRAF mutation, may be an important step in PTC tumorigenesis and progression.
- In idiopathic pulmonary fibrosis tissues TIMP3 gene expression was increased and the protein was localized to fibroblastic foci and extracellular matrix. Our findings suggest that TGF-beta1-induced TIMP3 may be an important mediator in lung fibrogenesis.
- A novel mutation in TIMP3 causes a late-onset form of SFD (Sorsby fundus dystrophy) in this family.
- TIMP-3 has a role in the pericyte-induced stabilization of newly formed vascular networks that are predisposed to undergo regression and reveal specific molecular targets of the inhibitors regulating these events.
- We observed a moderately increased risk for breast cancer in the C allele carriers of the TIMP3-1296 T/C SNP (OR 1.25, 95% CI 1.05-1.50)
- APMCF1 participates at least partially in cell cycle regulation through regulating genes such as p21 and TIMP3.
- TIMP2 and TIMP3 play functional role in LPA-induced invasion as negative regulators.
- TIMP-3 interacts with the ECM via both its N- and C-terminal domains. The amino acids involved in ECM binding are all basic in nature: Lys-26, Lys-27, Lys-30, Lys-76 of the N-terminal domain and Arg-163, Lys-165 of the C-terminal domain
- Only p16 (INK4A )and TIMP3 were methylated consistently in medulloblastomas (p16 (INK4A ) 14%, TIMP3 11%) and p16 (INK4A) also in anaplastic ependymomas (1/4 tumors).
- TIMP3, DAPK1 and AKR1B10 are important for squamous cell lung cancer tumorogenesis while AKR1B10 is potential oncogene whereas TIMP3 and DAPK1 are potential tumor suppressor genes.
- Requirement of PI3K signaling pathway for regulation of TIMP3 gene expression by TGFbeta in chondrocytes.
- TIMP-3 inhibition of ADAMTS-4 is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4
- Increased mesenchymal stem cell culture confluence impairs migration and is related to an upregulation of TIMP-3.
- TIMP-3 promoter hypermethylation is elevated in HNSCC and is highly correlated with DAPK hypermethylation, implying a functional relationship between these genes.
- attenuated expression of TIMP3 may play an important role in genesis and development of colon carcinoma
- TIMP3 is uniquely regulated by Oxidised, glycated LDL lipoproteins, which may contribute to microvascular abnormalities in diabetic retinopathy.
- upregulation of TIMP-3 expression in HCC-7721 cells inhibits invasion capacity in vitro as well as tumorigenic and metastatic potential in nude mice.
- Genetic changes in the timp-3 gene (TIMP-3) lead to a shift towards the myofibroblast phenotype in the fibroblast culture.
- Acrolein, a constituent of cigarette smoke and an endogenous mediator of oxidative stress, decreases Timp3 mRNA in mouse lung.
- Methylation and loss of expression of TIMP3 occurs infrequently in esophageal squamous cell carcinoma in a region of high incidence in China
- TIMP-1, -2, and -3 are significantly reduced by chorionic gonadotropin in endometrial stromal cells.
- TIMP-3 is an upstream mediator of neuronal apoptosis and likely contributes to neuronal loss in neurodegenerative diseases such as amyotrophic lateral sclerosis.
- In the presence of TIMP-3 and AGTR2, vascular endothelial growth factor-induced human umbilical vein endothelial cell proliferation was additively inhibited.
- IL-10 further regulates TNF-alpha by modulating TACE activation at early time points and by contributing to the induction of TIMP-3, the natural inhibitor of active TACE, at later time points
- Results suggest that receptor-activated Smad2 and Smad3 and co-Smad4 critically mediate TGF-beta-stimulated TIMP-3 expression in human chondrocytes and TIMP-3 gene is a target of Smad signaling pathway.
- there is frequent TIMP-3 promoter methylation in adenocarcinomas of the esophagus and stomach
- TIMP-3 is downregulated in a distinct subpopulation of atherosclerotic foam cells which have increased MMP-14.
- The combination of favourable functional epitopes together with a considerable flexibility renders TIMP-3 an efficient TACE inhibitor.
- TIMP-3 protein accumulation was found to be an age-dependent phenomenon.
- TIMP-3 hypermethylation is associated with lower TIMP-3 protein expression in esophageal squamous cell carcinoma and with poor patient survival due to a high frequency of recurrence by pleural dissemination
- Data showed that ADAM17 and its specific inhibitor TIMP3 were co-expressed in the human intestinal barrier and ADAM17 inhibition, either physiologically or pharmacologically, amplified TNF-alpha-mediated hyperpermeability.
- of promoter hypermethylation of TIMP3, CDH1, DAPK, RASSF1A, p16INK4A and MGMT, only the epigenetic silencing of TIMP3 and CDH1 predicted a better outcome in head and neck squamous cell carcinoma