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23-024 p27 Protein complex, activated, 10 µg

Activated complex of three (3) full length, recombinant human proteins: p27, Cyclin E1, & CDK2. Phosphorylated in vitro using CDK2/Cyclin E1. For use in Enzyme Assays. Behaves as a substrate in ubiquitin assays.

p27 Protein complex, activated, 10 µg MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
Key Applications: Enzyme Assays
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23-024
10 µg  
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Overview

Replacement Information

Key Spec Table

Key ApplicationsSpeciesCascade Component
Enzyme AssaysHuman Substrate
Description
Catalogue Number23-024
Brand Family Upstate
Trade Name
  • Upstate
Descriptionp27 Protein complex, activated, 10 µg
OverviewC-terminal cMyc and 6His-tagged, recombinant human Smac/DIABLO amino acids 56-end, expressed in E.coli
Alternate Names
  • p27kip1
  • Cyclin-dependent kinase inhibitor 1B
  • Kip1
Background Informationp27 is an important regulator of cell cycle progression, involved in G1 arrest. It is a potent inhibitor of cyclin E1- and cyclin A-CDK2 complexes and a positive regulator of cyclin D-dependent kinases such as CDK4. The degradation of this protein, which is triggered by its CDK-dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state. Decreased levels of p27 are found in various epithelial tumours originating from lung, breast, colon, ovary, oesophagus, thyroid and prostate. Defects in the gene encoding p27 (CDKN1B) are the cause of multiple endocrine neoplasia type 4 (MEN4) an inherited cancer of the thyroid.
References
Product Information
Quality LevelMQ100
Applications
ApplicationActivated complex of three (3) full length, recombinant human proteins: p27, Cyclin E1, & CDK2. Phosphorylated in vitro using CDK2/Cyclin E1. For use in Enzyme Assays. Behaves as a substrate in ubiquitin assays.
Key Applications
  • Enzyme Assays
Biological Information
Specific ActivityFor Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Cascade ComponentSubstrate
Entrez Gene Number
Purification MethodPurified using immobilized metal affinity chromatography.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
  • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Packaging Information
Material Size10 µg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
23-024 04053252294693

Documentation

p27 Protein complex, activated, 10 µg SDS

Title

Safety Data Sheet (SDS) 

p27 Protein complex, activated, 10 µg Certificates of Analysis

TitleLot Number
p27 complex, activated (Recombinant protein expressed in Sf21 insect cells) - Dl1DP017NB D11DP017NB
p27 complex, activated - D11EP028N-A D11EP028N-A
p27 complex, activated - D11EP028NA D11EP028NA
p27 complex, activated - D11EP028NB D11EP028NB
p27 complex, activated - Dl1DP017NB DL1DP017NB

Technical Info

Title
Detecting Substrate Ubiquitination by the E3 Ligase, XIAP, Using Quantitative Assays

Related Products & Applications

Alternative Packsize

Catalogue Number Description
23-024M p27 Protein complex, activated, 250 µg

Product Families

Ubiquitin Proteasome System: Enzymes and Substrates

Millipore has removed the complexity of Ubiquitination by providing functionally validated enzymes and substrates, making the pathway readily accessible for research and drug discovery.
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Categories

Life Science Research > Drug Discovery and Development > Ubiquitin and Proteasome Screening > Ubiquitination Substrates
Life Science Research > Proteins and Enzymes > Substrate & Control Proteins > Ubiquitination Substrates