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Validated All-in-One™ qPCR Primer for FURIN(NM_002569.3) Search again
Product ID:
HQP012121
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
FUR, PACE, PCSK3, SPC1
Gene Description:
furin, paired basic amino acid cleaving enzyme
Target Gene Accession:
NM_002569.3(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
The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. Some of its substrates are: proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor. It is also thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140. This gene is thought to play a role in tumor progression. The use of alternate polyadenylation sites has been found for this gene.
Gene References into function
- we investigated the specificity and potency of complete prodomains and short C-terminal prodomain peptides of each SPC on highly purified, soluble enzyme preparations of human SPC1, SPC6, and SPC7.
- Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase
- results show that shedding of furin occurs rapidly and further suggest that specific cysteine residues may impart a conformation to the enzyme, thereby affecting its susceptibility to proteolysis
- involvement of the proximal GATA recognition motif in the P1 promoter and impact on the maturation of furin substrates of Furin gene regulation in differentiating megakaryoblastic cells.
- Increased activity of this enzyme enhances the malignant phenotype of human head and neck cancer cells.
- role in Semliki Forest virus p62 processing
- furin has a role in processing human pro-CNP
- Data suggest that mutations that diminish domain 2 Ca(2+) binding allow furin access to an otherwise protected cleavage site, initiating the proteolytic cascade that leads to gelsolin amyloidogenesis and familial amyloidosis of Finnish type.
- findings established the existence of a novel alternative/complementary pathway by which furin increases tumor cell invasion through an amplification/activation loop between MMP-2 and TGFbeta
- furin is a novel chemokine-modifying enzyme in vitro and most probably also in vivo, generating a C-terminally truncated CXCL10, which fully retains its (inverse) agonistic properties.
- modelling of furin's pro-region revealed that Ile-60 and His-66 might be crucial in forming the binding interface with the catalytic domain, while residues Trp-34 and Phe-67 might be involved in maintaining a hydrophobic core within the pro-region itself
- furin is responsible for VEGF-C processing in human oral tongue squamous cell carcinoma progression
- Results report the identification of Spn4A, a previously uncharacterized secretory pathway serine protease inhibitor (serpin) from Drosophila melanogaster that contains a consensus furin cleavage site.
- HIV-1 gp160 processing by furin is inhibited by polyarginine
- releases Feline foamy virus (FFV) Env leader protein (Elp)from ENV precursor protein.
- HGF and BCL-2 family proteins use a furin-dependent pathway to promote invasion via TGF-beta and MMP in human malignant glioma cells and the pro-invasive properties of TGF-beta require furin- dependent MMP activity.
- From a brain cDNA library of possible interacting proteins, furin efficiently processes both the beta-secretase beta-amyloid protein converting enzyme pro-BACE1 and its novel interacting partner brain-specific type II membrane protein pro-BRI3.
- Analysis of furin promoters revealed the presence of putative binding sites for HIF-1; hypoxic/HIF-1 regulation of furin correlated with increased proteolytic activation of substrates MMP1 and TFGbeta1.
- furin can directly cleave the RXXR amino acid sequence in the propeptide domain of proMMP-2 leading to inactivation of the enzyme.
- serpin/furin complex stability depends on pH and regulation at the deacylation step
- furin and PC5 play a role in a MT-MMP-MMP-2 proteolytic cascade, involving provision of macrophage MT1-MMP for the activation of pro-MMP-2; furin and PC5 are expressed in monocytes and colocalize with MT1-MMP in macrophages in the atherosclerotic plaque
- an amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward furin
- pro-ADAMTS9 is processed at the cell surface by furin
- IL-12 caused Furin to be preferentially expressed in differentiated Th1 cells in a Stat4-dependent manner
- Furin mediates cleavage of a receptor tyrosine phosphatase and regulation of beta catenin's transcriptional activity.
- PCSK9 levels are finely regulated by the basic amino acid convertases furin and PC5/6A
- furin enhances alpha-secretase activity via the cleavage of ADAM10 and TACE, and attenuated furin activity is connected to the production of Abeta
- These findings highlight a pivotal role for furin, MT1-MMP, and MMP2 in TNF-alpha-induced sphingolipid signaling, and they identify this system as a possible target to inhibit SMC proliferation in vascular diseases.
- Furin P1A promoter undergoes transactivation via Sox9 binding during chondrogenesis.
- This study provides valuable insights into the structural properties of the furin prodomain in relation to its role in the folding of the furin zymogen and its inhibitory action toward furin.
- Furin may constitute a marker for ovarian tumor progression and could contribute to predict the outcome of this disease.
- HEPC MISSENSE MUTATION CAUSING INEFFICIENT CLEAVAGE INDICATES THAT THE FURIN BINDING SITE BE MORE THAN 4 RESIDUES
- the hepatic prohormone convertase furin mediates the posttranslational processing of hepcidin. The proteolytic cleavage of prohepcidin to hepcidin is not regulated by iron-transferrin or the HIF pathway
- ppFurin expression in breast cancer cells decreased MMP-9 activity, but had no significant effect on TIMP-1 secretion.
- s-HJV originates from a furin cleavage at position 332-335
- Data suggest that furin levels in cystic fibrosis respiratory epithelial cells contributes to bacterial toxin-induced cell death, fibrosis, and local immunosuppression.
- These data support the hypothesis of a direct binding of heparin with site1 and site2, allowing selective exposure/accessibility of the REKR sequence, which is only then optimally cleaved by furin.
- PC furin is a major IGF-1 receptor convertase.
- The Ca2+-binding capacity of epidermal furin is disrupted by H2O2-mediated oxidation in vitiligo.
- fibrates simultaneously decreased PCSK9 expression while increasing PC5/6A and furin expression, indicating a broad action of PPARalpha activation in proprotein convertase-mediated lipid homeostasis.
- CysLT1 is involved in remodeling processes through modulation of furin transcription.
- T(3) regulates furin gene expression via a novel mechanism or in cooperation with TGF-beta to enhance tumor metastasis in vitro and in vivo.
- the interaction between the PTB domain of Mint3 and the acidic peptide signal of Furin regulates the specific localization of Furin in the trans-Golgi network
- Proteomic profiling of CHO cells with enhanced rhBMP2 productivity following co-expression of furin is reported.
- Activin stimulates endogenous inhibin alpha- and betaB-subunit mRNA, protein, and proteolytic processing. Simultaneously, activin stimulated the proconvertase furin through a Smad2/3-dependent process.
- level of furin expression in Colo16 cells correlated to changes in pp38 levels in the cells following exposure to UV radiation