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Validated All-in-One™ qPCR Primer for SIAH2(NM_005067.6) Search again
Product ID:
HQP017163
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
hSiah2
Gene Description:
siah E3 ubiquitin protein ligase 2
Target Gene Accession:
NM_005067.6(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:
Summary
This gene encodes a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific proteins. The activity of this ubiquitin ligase has been implicated in regulating cellular response to hypoxia.
Gene References into function
- SIAH2 regulates the expression of promyelocytic leukemia protein and other tripartite motif proteins
- SIAH2 regulates stability of prolyl- hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia.
- role of interaction with AF4 and AF4.MLL fusion protein in t(4,11) pathobiology
- 2-oxoglutarate (alpha-ketoglutarate) dehydrogenase stability is regulated by the RING finger ubiquitin ligase Siah
- mechanism by which the estrogen-ER complex markedly reduces the level of N-CoR through a process involving the up-regulation of Siah2 and the subsequent targeting of N-CoR for proteasomal degradation
- Association of two isoforms Siah1 and Siah2 results in the regulation of Siah1 stability by Siah2 in the presence of a ring finger domain in HEK293 cells.
- Mechanism underlying the regulation of PHD3 availability and activity in hypoxia by the E3 ligase Siah2.
- The role of Siah2 phosphorylation in the regulation of its activity toward PHD3 is reported.
- We provide evidences for hSiah2-dependent degradation of Pias as being a mechanism in the regulation of c-jun N-terminal kinase-activating pathways.
- Data show that Siah2 is an important mediator of repp86 protein degradation.
- monoubiquitylation by SIAH1 and SIAH2 represents a possible trigger event for alpha-synuclein aggregation and Lewy body formation
- SIAH-2 may be a viable target for novel anti-RAS and anticancer agents aimed at inhibiting EGFR and/or RAS-mediated tumorigenesis.
- Hypoxic conditions allow a markedly increased HIPK2/Siah2 interaction and result in efficient polyubiquitylation and proteasomal degradation of the kinase.
