Recombinant Human CK2 alpha 1 Protein

Name: Recombinant Human CK2 alpha 1 Protein
Brand: Beta LifeScience
SKU: BL-0818SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_001895
Synonym	CKII; CK2A1; CKIIalpha; CSNK2A1
Background	CK2alpha is a serine-threonine protein kinase whose targets include many critical regulators of cellular growth. It is highly expressed in a lymphopro-liferative disease of cattle and in many human cancers. Overexpression of the CK2 catalytic subunit in lymphocytes of transgenic mice leads to T cell lymphoma (1). The highest CK2alpha1 activity is found in mouse testicles and brain, followed by spleen, liver, lung, kidney and heart (2).
Description	Recombinant full-length human CK2alpha1 was produced by baculovirus in Sf9 insect cells using a N-terminual GST tag. This protein is purified with our unique purification methods. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~70 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human CK2 alpha 1 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue.
Subcellular Location	Nucleus.
Protein Families	Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
Database References	HGNC: 2457 OMIM: 115440 KEGG: hsa:1457 STRING: 9606.ENSP00000217244 UniGene: PMID: 28623166 Our results showcase the potentially valuable functional impact of microRNAs in regulating GG related epilepsy. As CK-2alpha inhibition enhances miR-217 expression, disrupting the miR-217-CK-2alpha interplay through CK-2alpha inhibitors might represent a novel therapeutic strategies aimed at LEAT. PMID: 28840260 The results suggest that CK2alpha promotes migration and invasion of clear cell renal cell carcinoma and therefore could serve as a novel prognostic biomarker and molecular therapeutic target in this type of cancer. PMID: 27906674 The newly designed casein kinase 2 (CK2) Inhibitors were screened on one lung cancer cell line A549, showing low micromolar anti-proliferative activity. PMID: 27491649 CK2 governs the molecular decision between encephalitogenic TH17 cells and protective Treg cells development. PMID: 27555590 Data suggest that casein kinase 2 (CK2) inhibition is a promising approach to blocking beta-catenin in MPNST cells, although combinatorial therapies may be required for maximal efficacy. PMID: 27448963 Results provide evidence that CK2A is critical fro RSV virus replication in human cells. PMID: 27464690 Vascular smooth muscle protein kinase CK2 inhibition suppresses neointima formation via a proline-rich homeodomain-dependent mechanism. PMID: 28927755 we have identified kinases, particularly CK2, associated with the autocrine malignant cell network that may play a central role in sustaining the cytokine network and/or mediating its effects in ovarian cancer. PMID: 26871292 CK2 and AKT display a high degree of cross-regulation of their respective functions, both directly, through physical interaction and phosphorylation, and indirectly, through an intense cross-talk of key downstream effectors, ultimately leading to sustained AKT activation. (Review) PMID: 28373060 Phosphorylation of Ikaros by CK2 impairs Ikaros DNA-binding ability, as well as Ikaros ability to regulate gene expression and function as a tumor suppressor in leukemia. (Review) PMID: 27666503 data implicate CK2 as a regulator of the Th17/Treg axis and Th17 cell maturation and suggest that CK2 could be targeted for the treatment of Th17 cell-driven autoimmune disorders. PMID: 28468969 This study demonstrates that CSNK2A1 and SIRT6 are indicators of poor prognosis for breast carcinomas and that CSNK2A1-mediated phosphorylation of SIRT6 might be involved in the progression of breast carcinoma. PMID: 27746184 Our results disclose a novel interplay between ubiquitin- and phosphorylation-dependent signalling, and represent the first report of a regulatory mechanism for UIM-dependent function. They also suggest that CK2 inhibitors could release the full neuroprotective potential of HSJ1, and deserve future interest as therapeutic strategies for neurodegenerative disease. PMID: 28031292 CK2 inhibition in monocyte-derived dendritic cells led to an enhanced Th2 polarization in the absence of contact sensitizer stimulation. PMID: 27707883 In the present work we have shown a key role for protein kinase CK2 in promoting LSC survival through the modulation of the STAT3, NF-kappaB and AKT/FOXO signaling pathways. We have also shown that CK2 inactivation makes LSCs more sensitive to the chemotherapeutic drug doxorubicin. PMID: 27479180 our findings establish an important regulatory role of CK2alpha on BMI1 phosphorylation and stability and implicate the CK2alpha/BMI1 axis in ovarian cancer. PMID: 28270146 The lack of intermediate species of CK2 alpha2beta2 in solution suggests that the holoenzyme is a strong/stable multimeric complex that does not spontaneously dissociate; a considerable amount of monomer, the active form of CK2, is present in low ionic strength solutions. Multimer assembly appears driven by electrostatic interactions between the CK2alpha P+1 loop and the CK2beta acidic loop. PMID: 28572157 These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1. PMID: 27920254 The invasion and migration of A549 cells were significantly inhibited after the knockdown of CK2alpha expression. PMID: 28442011 Somatic mutations in CSNK2A1 have been implicated in various cancers; however, this is the first study to describe a human condition associated with germline mutations in any of the CK2 subunits PMID: 27048600 This study shows for the first time that LPS inhibits colonic biotin uptake via decreasing membrane expression of its transporter and that these effects likely involve a CK2-mediated pathway. PMID: 28052864 This study indicates that CKII can modulate the intracellular reactive oxygen species level via FoxO3a. PMID: 27470586 Twelve SNPs from four regions were significantly associated with aggressive disease, among which, three linked SNPs in CSNK1A1 at 5q32 (represented by rs752822) may differentiate GS 4+3 from GS 3+4 patients (OR = 1.44, 95% CI = 1.12-1.87, P = 4.76x10(-3)). PMID: 27515962 using a kinase-inactive mutant of CK2alpha, that RAF-MEK inhibitor resistance did not rely on CK2alpha kinase catalytic function, and both wild-type and kinase-inactive CK2alpha maintained ERK phosphorylation upon inhibition of BRAF or MEK. PMID: 27226552 Inhibition of CK2 increased the expression of metabolic regulators, PDK4 and AMPK along with the key cellular energy sensor CREB. PMID: 27001465 Report provides evidence that CSNK2A1 kinase hyperactivity occurs in vivo in all classes of glioblastomas independently of TP53 status as well as in glial tumors of lower grades and histology. PMID: 27098015 CK2-increased ECE-1c protein stability is related to augmented migration and invasion of colon cancer cells, shedding light on a novel mechanism by which CK2 may promote malignant progression of this disease. PMID: 26543229 This study report increased levels of CK2 in the hippocampus and temporal cortex of AD patients compared to non-demented controls. PMID: 26732432 CK2-mediated phosphorylation of ARC contributed to chemotherapy resistance by inhibiting DOX induced apoptosis; combining DOX with CK2 inhibitor could induce apoptosis of cancer cells synergistically by down-regulating the phosphorylation of ARC PMID: 26172393 Protein kinase CK2 expression predicts relapse survival in ERalpha dependent breast cancer, and modulates ERalpha expression in vitro. PMID: 26703694 Data suggest that complexes of HDAC3-H1.3 with NCOR1 and NCOR2/SMRT accumulate on chromatin in synchronized HeLa cells in late G2 phase and mitosis; deacetylation activity of HDAC3 is activated via phosphorylation of Ser-424 by CK2 only in mitosis. PMID: 26663086 ATG16L1 as a bona fide physiological CSNK2 and PPP1 substrate, which reveals a novel molecular link from CSNK2 to activation of the autophagy-specific ATG12-ATG5-ATG16L1 complex and autophagy induction PMID: 26083323 Data suggest that cryptochromes mediate periodic binding of Ck2b (casein kinase 2beta) to Bmal1 (aryl hydrocarbon receptor nuclear translocator-like protein) and thus inhibit Bmal1-Ser90 phosphorylation by Ck2a (casein kinase 2alpha). [SYNOPSIS] PMID: 26562283 The combination treatment of TRAIL and the CK2 inhibitor decreased p65 nuclear translocation... the treatment of a sub-dose of TRAIL, downregulation of CK2, using both genetic and pharmacological approaches . PMID: 26165401 our findings provide new insights on the potential relevance of the CK2-mediated phosphorylation of B23/NPM in cancer cells, revealing at the same time the potentialities of its pharmacological manipulation for cancer therapy PMID: 25805179 Inhibition of ecto-CK2 by K137-E4 is accompanied by a slower migration of cancer cells as judged by wound healing assays PMID: 26349539 CK2 is widely expressed in follicular, Burkitt and diffuse large B-cell lymphomas and may have role in malignant B-cell growth. PMID: 25788269 High casein kinase II expression is associated with B-cell acute lymphoblastic leukemia. PMID: 26219304 Data show that casein kinase 2 (CK2)-mediated phosphorylation of deubiquitylating enzyme OTUB1 at Ser16 causes nuclear accumulation of OTUB1. PMID: 25872870 Overall results, confirm that a balance of hydrophobic and electrostatic interactions contribute predominantly relative to possible intermolecular halogen/hydrogen bonding ,in binding of halogenated benzotriazoles to the ATP-binding site of hCK2alpha PMID: 25891901 These phosphopeptides include altogether 69 phosphoresidues, a large proportion of which (almost 50%) are generated by CK2, while the others do not conform to the CK2 consensus PMID: 25882195 Over-expressed CK2alpha positively regulate Hh/Gli1 signaling in human mesothelioma. PMID: 25422081 CDK11 and CK2 expression are individually essential for breast cancer cell survival, including TNBC. PMID: 25837326 There is a major role of the CK2alpha-interacting protein CKIP-1 in activation of PAK1 for neoplastic prostate cells transformation. PMID: 26160174 Casein kinase 2-mediated phosphorylation of Hsp90beta and stabilization of PXR is a key mechanism in the regulation of MDR1 expression. PMID: 25995454 Phosphorylation of KCNQ2 and KCNQ3 anchor domains by protein kinase CK2 augments binding to AnkG. PMID: 25998125 Results show that CK2alpha may have an important role in brain tumor-initiating cell maintenance through the regulation of beta-catenin in glioblastoma. PMID: 25241897 CK2-phosphorylation of eIF3j at Ser127 promotes the assembly of the eIF3 complex, a crucial step in the activation of the translation initiation machinery. PMID: 25887626 CK2 phosphorylates and inhibits TAp73 tumor suppressor function to promote expression of cancer stem cell genes and phenotype in head and neck cancer. PMID: 25379016

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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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