Recombinant Human CDK2 Protein (N-6His)

Name: Recombinant Human CDK2 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1278NP
Availability: InStock

BL-1278NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

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Product Overview

Description	Recombinant Human Cyclin-Dependent Kinase 2 is produced by our E.coli expression system and the target gene encoding Met1-Leu298 is expressed with a 6His tag at the N-terminus.
Accession	P24941
Synonym	Cyclin-Dependent Kinase 2; Cell Division Protein Kinase 2; p33 Protein Kinase; CDK2; CDKN2
Gene Background	Cyclin-dependent kinase 2 (CDK2) belongs to the cyclin-dependent kinase of Ser/Thr protein kinase. CDK2 acts as a catalytic subunit of the cyclin dependent kinase complex, whose activity is restricted to the G1-S phage of the cell cycle, it is essential for the G1/S transition. The kinase activity of CDK2 can be regulated by the association with a cyclin subunit, its phosphorylation state and CDK inhibitors. The activation of the CDK2/cyclin complex requires the phosphorylation of Thr160 and the dephosphorylation of Try14 and Tyr15. The inhibition of CDK2-cyclin complex can also be attributed to association with p27Kip1 and p21Waf1/Cip1. The activation of CDK2 has been shown to be necessary for apoptosis of quiescent cells, such as neurons, thymocytes and endothelial cells.
Molecular Mass	36.1 KDa
Apmol Mass	34 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 200mM NaCl, 1mM DTT, 40% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1. Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability. Phosphorylates CDK2AP2. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks.
Subcellular Location	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus, Cajal body. Cytoplasm. Endosome. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3).
Protein Families	Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
Database References	HGNC: 1771 OMIM: 116953 KEGG: hsa:1017 STRING: 9606.ENSP00000266970 UniGene: Hs.19192

Gene Functions References

Results indicate that although PIN1 increases p27 levels, it also attenuates p27's inhibitory activity on CDK2 and thereby contributes to increased G1-S phase transitions and cell proliferation. PMID: 29118189
CDK2 mutation is not associated with non-obstructive azoospermia. PMID: 29373224
Proteomics and phosphoproteomics analyses identified CDK2 as a driver of resistance to both BRAF and Hsp90 inhibitors and its expression is regulated by the transcription factor MITF upon XL888 treatment of melanoma cells. PMID: 29507054
identified a new phosphorylation-based substrate recognition mechanism of PTPN12 by CDK2, which orchestrated signaling crosstalk between the oncogenic CDK2 and HER2 pathways PMID: 28842430
CDK2 gene is a strong candidate gene for type-2 diabetes. CDK2 gene is located in a risk area composed of 4 blocks in strong LD around the type-2 diabetes SNP rs2069408. CDK2 overexpression inhibits the association of insulin receptor to the microtubule components, tubulin alpha and tubulin beta. Physical association of the insulin receptor complex with CDK2 is inhibited by the expression of tyrosine phosphatase PTPLAD1. PMID: 30300385
Among these genes, STAT3 and CDK2 were significantly associated with recurrence. Further study suggested that inhibition of CDK2 reduced invasion of Pca cell lines. The invasion ability was rescued after reintroduction of CDK2. PMID: 29323532
The roles of the CDK2/SIRT5 axis in gastric cancer. PMID: 29896817
CDK2 may have key functions in neuroblastoma progression by regulating the expression of neoplastic genes. PMID: 29328425
The authors show that human Cyclin-Dependent-Kinases (CDKs) target the RAD9 subunit of the 9-1-1 checkpoint clamp on Thr292, to modulate DNA damage checkpoint activation. Thr292 phosphorylation on RAD9 creates a binding site for Polo-Like-Kinase1 (PLK1), which phosphorylates RAD9 on Thr313. PMID: 29254517
this study suggests that CDK2 and CDK9 are potential therapeutic targets in Neuroblastoma (NB) and that abrogating CDK2 and CDK9 activity by small molecules like dinaciclib is a promising strategy and a treatment option for NB patients PMID: 27378523
LINC00958 acts as an oncogenic gene in the gliomagenesis through miR-203-CDK2 regulation, providing a novel insight into glioma tumorigenesis. PMID: 29570358
These compounds bind CDK2/ Cyclin A, inhibit its kinase activity, compete with substrate binding, but not with ATP, and dock onto the T-loop of CDK2. The best compound also binds CDK4 and CDK4/Cyclin D1, but not CDK1. PMID: 28430399
CDK2 contributes to S81-AR phosphorylation and transactivation while CDK4 was not shown to be involved in this process. PMID: 29157894
Our findings provide a rationale for clinical use of Bcl-2 family inhibitors in combination with CDK2 inhibitors for treatment of Mcl-1-dependent colorectal tumours associated with expression of Bcl-2, Bcl-XL and Bcl-w proteins. In addition, we have shown potential of CDK2 inhibitors for treatment of tumours expressing R273H mutant p53. PMID: 29372687
CDK2 phosphorylates polyQ-AR specifically at Ser(96). Phosphorylation of polyQ-AR by CDK2 increased protein stabilization and toxicity and is negatively regulated by the adenylyl cyclase/protein kinase A signaling pathway in spinobulbar muscular atrophy. PMID: 28003546
Data show that Noxa-mediated MCL-1 phosphorylation and degradation is regulated by CDK2. PMID: 27166195
The upregulation of miR-302b reduced the expression of CDK2, and inhibited ERK signaling pathway, thereby inhibiting cell proliferation and G1/S phase conversion rate. PMID: 27465546
High CDK2 expression is associated with breast cancer. PMID: 28760857
Here, we introduce a transcriptional signature to specifically track CDK2 activity. It responds to genetic and chemical perturbations in the CDK-RB-E2F axis, correlates with mitotic rate in vitro and in vivo and reacts rapidly to changes in CDK2 activity during cell cycle progression PMID: 27819669
Here, we found that centrosomal protein of 76 kDa (Cep76), previously shown to restrain centriole amplification, interacts with cyclin-dependent kinase 2 (CDK2) and is a bona fide substrate of this kinase. Cep76 is preferentially phosphorylated by cyclin A/CDK2 at a single site S83, and this event is crucial to suppress centriole amplification in S phase PMID: 27065328
The authors find that Spy1 confers structural changes to Cdk2 that obviate the requirement of Cdk activation loop phosphorylation. PMID: 28666995
CDK2 serves as an important nexus linking primary beta-cell dysfunction to progressive beta-cell mass deterioration in diabetes PMID: 28100774
a SUMO-deficient Rb mutant results in reduced SUMOylation and phosphorylation, weakened CDK2 binding, and attenuated E2F-1 sequestration. PMID: 27163259
These two states are separated by different metastable states that share hybrid structural features with both forms of the kinase. In contrast, the CDK2/ANS complex landscape is compatible with a conformational selection picture where the binding of ANS in proximity of the alphaC helix causes a population shift toward the inactive conformation PMID: 27100206
Dsg2 knockdown arrests non-small cell lung cancer cell cycle progression via modulation of p27-CDK2 levels. PMID: 27629878
CDK2 protects podocytes from apoptosis and reduced expression of CDK2 associates with the development of diabetic nephropathy. PMID: 26876672
CDK2 controls a wide-spread epigenetic program that drives transcription at differentiation-related gene promoters specifically in G1. (Review) PMID: 26857166
SATB2 regulates the mitosis of cell cycle and affects G1 cell cycle via interaction with CDK2. PMID: 26714749
A novel link has been discussed between CDK2 expression and cell migration by characterizing the CDK2-mediated phosphorylation of BRMS1. PMID: 26730572
the results suggest that CK1delta activity can be modulated by the interplay between CK1delta and CDK2/E or CDK5/p35. PMID: 26464264
Inappropriate activation of CDK2 in S phase underlies the sensitivity of a subset of cell lines to Chk1 inhibitors. PMID: 26595527
CDK2 and DNA-PK regulate PR transcriptional activity by distinct mechanisms. PMID: 26652902
The expression of cdk2 in malignancy of ovarian tumors. PMID: 26828990
PHD1 is phosphorylated by CDK2, CDK4 and CDK6 at Serine 130. PMID: 26644182
Results show that miR-200c plays an antioncogenic role in clear cell renal cell carcinomas, through controlling cell growth and cell-cycle progression by downregulating the G1-S regulator CDK2. PMID: 26248649
show thata combining cyclin-dependent kinase 2 (CDK2) antagonism and ubiquitin thioesterase 33 (USP33) depletion augments anaphase catastrophe via changes in centrosomal protein of 110 kDa (CP110) protein expression. PMID: 26304236
Foxo3 circular RNA retards cell cycle progression via forming ternary complexes with p21 and CDK2. PMID: 26861625
our study reveals a novel function of CDK2 in EGF-induced cell transformation and the associated signal transduction pathways. This indicates that CDK2 is a useful molecular target for the chemoprevention and therapy against skin cancer. PMID: 26028036
both cell lines feature a significant reduction of CDK2 expression verified at the RNA and protein level, respectively PMID: 26555773
Centriolar satellites build a centrosomal microcephaly protein complex critical for human neurodevelopment that promotes CDK2 centrosomal localization and centriole duplication. PMID: 26297806
Identified ING5 as a novel CDK2 substrate. ING5 is phosphorylated at a single site, threonine 152, by cyclin E/CDK2 and cyclin A/CDK2. This site is also phosphorylated in cells in a cell cycle dependent manner, consistent with it being a CDK2 substrate. PMID: 25860957
fluspirilene is a potential CDK2 inhibitor and a candidate anti-cancer drug for the treatment of human hepatocellular carcinoma. PMID: 26147897
analysis of the conformational characteristics and ligand binding mechanisms of CDK2 [review] PMID: 25918937
Which is mutated at the CDK2 phosphorylation site. PMID: 25154617
observations suggested that androgen suppresses the proliferation of CRPC cells partially through inhibition of Cyclin A, Cdk2, and Skp2 PMID: 25271736
A positive correlation between cdk2/cyclin A expression level and tumor growth. Amygdalin, therefore, may block tumor growth. PMID: 25136960
Report structure-based discovery of allosteric inhibitors of CDK2. PMID: 24911186
Sox2 phosphorylation by Cdk2 promotes the establishment but not the maintenance of the pluripotent state. PMID: 26139602
Inhibition of CDK2 phosphorylation blocked phosphorylation of hnRNP K, preventing its incorporation into stress granules (SGs). Due to interaction between hnRNP K with TDP-43, the loss of hnRNP K from SGs prevented accumulation of TDP-43. PMID: 25410660
The docking and molecular dynamics investigation performed here led to the identification of the interactions responsible for stabilizing the ligand ChEMBL474807 at the active sites of the glycogen synthase kinase-3beta (GSK-3) and cyclin-dependent kinase-2 PMID: 25754137

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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