SRP5109
p27KIP1, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
CDKN1B, CDKN4, MEN1B
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About This Item
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biological source
human
recombinant
expressed in E. coli
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~52 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CDKN1B(1027)
General description
KIP1 (cyclin-dependent kinase inhibitor 1B) is a kinesin-related motor protein required for mitotic spindle assembly and chromosome segregation. Many tumorigenic processes modulate cell-cycle progression by regulating the levels of the cyclin-dependent kinase inhibitor KIP1. KIP1 binds to and inhibits cyclinE-Cdk2 complex, cyclinA-CDK2 and cyclinD1-CDK4. The phosphorylation- and ubiquitination-dependent proteolysis of KIP1 is implicated in control of the G1-S transition in the cell cycle. KIP1 is critical for retinoblastoma protein (Rb)-induced cellular proliferative senescence.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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M A Hoyt et al.
The Journal of cell biology, 118(1), 109-120 (1992-07-01)
Two Saccharomyces cerevisiae genes, CIN8 and KIP1 (a.k.a. CIN9), were identified by their requirement for normal chromosome segregation. Both genes encode polypeptides related to the heavy chain of the microtubule-based force-generating enzyme kinesin. Cin8p was found to be required for
A C Carrano et al.
Nature cell biology, 1(4), 193-199 (1999-11-13)
Degradation of the mammalian cyclin-dependent kinase (CDK) inhibitor p27 is required for the cellular transition from quiescence to the proliferative state. The ubiquitination and subsequent degradation of p27 depend on its phosphorylation by cyclin-CDK complexes. However, the ubiquitin-protein ligase necessary
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