CDK1 Protein, Human (Inactive, sf9, GST)
Based on 1 Customer Validation
The CDK1/CDC2-cyclin-B complex is a key regulator in the cell cycle. It plays an important role in cell division and development and regulates a variety of cellular activities, including chromosome segregation, nuclear membrane rupture, cytokinesis, etc. The activity of CDK1 is regulated by a variety of phosphorylation and dephosphorylation, thereby controlling the progression of the cell cycle and the DNA repair process. CDK1 Protein, Human (sf9, GST) is the recombinant human-derived CDK1 protein, expressed by Sf9 insect cells , with N-GST labeled tag.
- Species: Human
- Source: Sf9 insect cells
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- Help & FAQs
Biological Activity
Description
The CDK1/CDC2-cyclin-B complex is a key regulator in the cell cycle. It plays an important role in cell division and development and regulates a variety of cellular activities, including chromosome segregation, nuclear membrane rupture, cytokinesis, etc. The activity of CDK1 is regulated by a variety of phosphorylation and dephosphorylation, thereby controlling the progression of the cell cycle and the DNA repair process. CDK1 Protein, Human (sf9, GST) is the recombinant human-derived CDK1 protein, expressed by Sf9 insect cells , with N-GST labeled tag.
Background
The CDK1/CDC2-cyclin-B complex is a key regulator of the cell cycle. It plays an important control role in the interphase fertilized egg and is crucial for the early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates the CDK1/cyclin complex. This complex phosphorylates multiple substrates, triggering centrosome dissociation, Golgi dynamics, nuclear envelope disruption, and chromosome condensation. After chromosomes are condensed and aligned on the metaphase plate, CDK1 activity is turned off by WEE1- and PKMYT1-mediated phosphorylation, allowing sister chromatid separation, chromosome decondensation, nuclear envelope remodeling, and cytokinesis. When DNA is damaged, CDK1 will be inactivated by phosphorylation mediated by PKR/EIF2AK2 and WEE1, thereby stopping the cell cycle and genome replication and promoting DNA repair. After repair is completed, CDK1 is reactivated by WIP1-dependent signaling to resume cell cycle progression. In proliferating cells, CDK1-mediated phosphorylation can inhibit FOXO1 interactions and promote FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. In addition, phosphorylation of CDK1 can also regulate microtubule dynamics, spindle formation and other processes.
Verified Bioactivity
The product demonstrated no detectable kinase activity in an ATP/ADP-based kinase assay.
Technical Parameters
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Species Human
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Source Sf9 insect cells
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Tag N-GST
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Accession
P06493 (M1-M297)
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Molecular Construction
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N-term
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GST
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CDK1 (M1-M297)
Accession # P06493 -
C-term
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Protein Length
Full Length
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Synonyms
CDK1; Cell Division Protein Kinase 1; Prev. CDC2; P34 Protein Kinase; CDC28A; P34CDC2; Cell Division Cycle 2, G1 To S And G2 To M; Cell Cycle Controller CDC2; Cell Division Control Protein 2 Homolog; CDKN1; Cyclin Dependent Kinase 1; Cyclin-Dependent Kina
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AA Sequence
MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM
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Predicted Molecular Mass
60 kDa
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Molecular Weight
Approximately 53 kDa, based on SDS-PAGE under reducing conditions.
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Glycosylation
Yes
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Purity
≥ 80%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.22 μm filtered solution of 50 mM Tris, 100 mM NaCl, 0.5 mM PMSF, 0.5 mM EDTA, 0.5 mM GSH, pH 8.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (237 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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