Recombinant Human CyclinK Protein

Name: Recombinant Human CyclinK Protein
Brand: Beta LifeScience
SKU: BL-1554SG
Availability: InStock

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

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Product Overview

Tag	GST
Host Species	Human
Accession	BC015935
Synonym	CCNK, CPR4, MGC9113
Background	CyclinK is a member of the cyclin family which can regulate transcription through their association with and activation of cyclin-dependent kinases (CDK). The CDK/CyclinK complex can phosphorylate the C-terminal domain (CTD) of the large subunit of RNA polymerase II (1). CyclinK is associated with potent CTD kinase and CDK kinase activities in vitro and coimmunoprecipitates with POLR2A. CyclinK is a new member of the transcription cyclin family which may play a dual role in regulating CDK and RNA polymerase II activities (2).
Description	Recombinant full-length human CyclinK was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~67 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
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 CyclinK 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	Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).
Subcellular Location	Nucleus.
Protein Families	Cyclin family, Cyclin C subfamily
Database References	HGNC: 1596 OMIM: 603544 KEGG: hsa:8812 STRING: 9606.ENSP00000374529 UniGene: PMID: 29760377 Cyclin K regulates prereplicative complex assembly to promote mammalian cell proliferation PMID: 29760377 Structures of CDK12/CycK complexes solved in the presence of AMP-PNP. PMID: 26597175 Data show that most mutations prevent formation of the cyclin-dependent kinase 12 (Cdk12)/cyclin K (CycK) complex, rendering the kinase inactive. PMID: 25712099 that cyclin K may be a novel molecular link between germ cell development, cancer development and embryonic stem cell maintenance. PMID: 25004108 Cyclin K is highly expressed in mammalian testes in a developmentally regulated manner. PMID: 25004108 Cyclin K interacts with CDK12 and CDK13 but not CDK9 in cells, and is required to maintain self-renewal in ES cells. PMID: 22547058 Cyclin K1 is the primary cyclin partner for CDK12/CrkRS and it is required for activation of CDK12/CrkRS to phosphorylate the C-terminal domain of RNA Pol II. PMID: 22988298 Cyclin K inhibits HIV-1 gene expression and replication by interfering with cyclin-dependent kinase 9 (CDK9)-cyclin T1 interaction in Nef-dependent manner. PMID: 21555514 These results reveal an unexpectedly direct role for CDK9-cyclin K in checkpoint pathways that maintain genome integrity in response to replication stress. PMID: 20930849 Cyclin K-expressing multiple myeloma LP-1 cells have lost their migration properties and display enhanced clonogenic capacities PMID: 20459741 P-TEFb containing cyclin K and Cdk9 can activate transcription via RNA. PMID: 11884399 cyclin K may play a role in regulating the cell cycle or apoptosis PMID: 11988847 The cyclin K fold comprises two typical cyclin boxes with two short helices preceding the N-terminal box. A prominent feature of cyclin K is an additional helix (H4a) in the first cyclin box that obstructs the binding pocket for the p27. PMID: 17169370

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.