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Validated All-in-One™ qPCR Primer for ISG15(NM_005101.2) Search again
Product ID:
HQP023013
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
G1P2, IFI15, IMD38, IP17, UCRP, hUCRP
Gene Description:
ISG15 ubiquitin like modifier
Target Gene Accession:
NM_005101.2(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
G1P2 is a ubiquitin-like protein that becomes conjugated to many cellular proteins upon activation by interferon-alpha (IFNA; MIM 147660) and -beta (IFNB; MIM 147640) (Zhao et al., 2005 [PubMed 16009940]).[supplied by OMIM].
Gene References into function
- The ISG15 gene contains a unique interferon-stimulated response element that enables the binding and recruiting not only of interferon regulatory factors but also of PU.1.
- Interferon stimulated gene 15 constitutively produced by melanoma cells induces e-cadherin expression on human dendritic cells.
- RA treatment of APL and other RA-responsive leukemic cells induced expression of UBE1L and ISG15 as well as intracellular ISG15 conjugates. A physical association was found between UBE1L and ISG15 in vivo.
- Quantitative-PCR and Northern analysis confirmed down-regulation of UCRP and UBE2L6 with BRCA2 knockdown, respectively.
- ISG15 is induced by camptothecin in human tumor cells
- The three-dimensional structure of recombinant ISG15C78S was determined at 2.4-A resolution.The docking model predicts side-chain interactions that presumably define the specificity between the ubiquitin and ISG15 ligation pathways
- ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways.
- identify Lys92 as the only ISG15 modification site in Ubc13, which is the first report about the ISG15 modification site
- These data indicate that ISGylation targets proteins found in several fundamentally important cellular pathways and will contribute to understanding the physiologic role of interferon-induced ISG15 and ISG15 conjugation.
- results suggest that the ISG15 pathway, which is deregulated during tumorigenesis, negatively regulates the ubiquitin/proteasome pathway by interfering with protein polyubiquitination/degradation
- ISG15 is the critical component in IFN-mediated inhibition of HIV-1 release
- Higher levels of ISG15 protein is associated with muscle-invasive bladder cancer
- Four candidate target proteins were demonstrated to be ISGylated in UBE1L- and UbcH8-dependent manners
- Efp protein could be conjugated with not only ubiquitin but also ISG15.
- review evidence of a role for ISG15 as an endogenous tumor suppressor that, when dysregulated in malignant cells, can be subverted to promote oncogenesis
- Thus we propose that autoISGylation of EFP negatively regulates its ISG15 E3 ligase activity for 14-3-3sigma.
- ISGylation (by ISG15) of 4EHP may play an important role in cap structure-dependent translation control in immune responses.
- Our results demonstrate that SARS-CoV PLpro can differentiate between ubiquitin-like modifiers sharing a common C-terminal sequence, and that the debranching activity of the PLpro is linkage type selective.
- a mechanistically novel function of ISG15 in the enhancement of the innate anti-viral response through specific inhibition of Nedd4 Ub-E3 activity
- These data provide evidence of antiviral activity of ISG15 against Ebola virus and suggest a mechanism of action involving disruption of Nedd4 function and subsequent ubiquitination of VP40.
- N-terminal ubiquitin-like domain of ISG15 mainly functions in the ligation step and Influenza B virus NS1 protein inhibits ISGylation by competing with E3 ligases for binding to the N-terminal domain
- These results suggest that ISG15, which interferes with proteasome-mediated repair of TOP1-DNA covalent complexes, is a potential tumor biomarker.
- Ube1L was required for transfer of ISG15 to UbcH8 and for binding of Ube1L to UbcH8
- nitrosylation of ISG15 enhances target protein ISGylation
- expression of the ISG15 system suppresses NF-kappaB activation
- Kinetic analysis revealed that mutation of arginine 153 to alanine (R153A) in ISG15 ablated hISG15-hUbE1L binding and transthiolation of UbcH8.
- UBE1L-ISG15 preferentially inhibits cyclin D1 in lung cancer