Recombinant Human SKP2 protein (GST tag N-Terminus)
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Recombinant Human SKP2 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 424 aa range, expressed in Wheat germ, with >80%, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
FBXL1, SKP2, S-phase kinase-associated protein 2, Cyclin-A/CDK2-associated protein p45, F-box protein Skp2, F-box/LRR-repeat protein 1, p45skp2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SKP2 protein (GST tag N-Terminus) (AB114385)
ab114385 analysed on a 12.5% SDS-PAGE Stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SKP2 is part of the SCF (SKP1-CUL1-F-box) complex which is instrumental in controlling cell cycle and cell division. It regulates the degradation of p27^Kip1 and other cell cycle regulators. By modulating proteolysis SKP2 contributes to the maintenance of cell proliferation and it has essential roles in cellular responses to growth signals. Moreover SKP2 influences processes such as DNA replication through its effect on substrate interaction and ubiquitination.
Pathways
SKP2 functions inside the ubiquitin-proteasome system and impacts the PI3K/AKT signaling pathway. SKP2 advances cell cycle progression by associating with proteins like p27^Kip1 and CDK2 facilitating cell division. It modulates the phosphorylation state of numerous targets influencing signaling processes that control cell growth. This involvement aligns SKP2 with key cellular pathways that maintain cell survival and metabolic balance.
Specifications
Form
Liquid
Additional notes
Glutathione Sepharose
General info
Function
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (PubMed : 11931757, PubMed : 12435635, PubMed : 12769844, PubMed : 12840033, PubMed : 15342634, PubMed : 15668399, PubMed : 15949444, PubMed : 16103164, PubMed : 16262255, PubMed : 16581786, PubMed : 16951159, PubMed : 17908926, PubMed : 17962192, PubMed : 22464731, PubMed : 22770219, PubMed : 32267835). Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition (By similarity). Degradation of CDKN1B/p27kip also requires CKS1 (By similarity). Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, NBN, FOXO1, UBP43, YTHDF2, and probably MYC, TOB1 and TAL1 (PubMed : 11931757, PubMed : 12435635, PubMed : 12769844, PubMed : 12840033, PubMed : 15342634, PubMed : 15668399, PubMed : 15949444, PubMed : 16103164, PubMed : 16581786, PubMed : 16951159, PubMed : 17908926, PubMed : 17962192, PubMed : 22464731, PubMed : 32267835). Degradation of TAL1 also requires STUB1 (PubMed : 17962192). Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2 (PubMed : 16262255). Promotes ubiquitination and destruction of CDH1 in a CK1-dependent manner, thereby regulating cell migration (PubMed : 22770219). Following phosphorylation in response to DNA damage, mediates 'Lys-63'-linked ubiquitination of NBN, promoting ATM recruitment to DNA damage sites and DNA repair via homologous recombination (PubMed : 22464731).. Through the ubiquitin-mediated proteasomal degradation of hepatitis C virus non-structural protein 5A, has an antiviral activity towards that virus.
Post-translational modifications
Phosphorylated on serine and threonine resudues in response to DNA damage, promoting 'Lys-63'-linked ubiquitination of NBN.. Ubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Deubiquitinated by USP13.. Acetylation at Lys-68 and Lys-71 increases stability through impairment of APC/C-mediated proteolysis and promotes cytoplasmic retention. Deacetylated by SIRT3.
Subcellular localisation
Nucleus
Target data
Product promise
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