Recombinant Human CDKN3 Protein

Name: Recombinant Human CDKN3 Protein
Brand: Beta LifeScience
SKU: BL-1546SG
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_005192
Synonym	CDI1, CIP2, FLJ25787, KAP, KAP1, MGC70625
Background	CDKN3 is a member of the dual specificity protein phosphatase family that acts as a cyclin-dependent kinase inhibitor (1). CDKN3 has been shown to interact with and dephosphorylate specifically the CDK2 kinase thereby preventing it's activation. CDKN3 has been reported to be deleted, mutated, or overexpressed in several kinds of cancers. Increased expression of CDKN3 leads to increased levels of kinase-associated phosphatase activity that inhibits the G(1)/S transition of the cell cycle by dephosphorylating the cyclin-dependent kinases (2).
Description	Recombinant full-length human CDKN3 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	~51 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 CDKN3 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	May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner.
Subcellular Location	Cytoplasm, perinuclear region.
Protein Families	Protein-tyrosine phosphatase family
Database References	HGNC: 1791 OMIM: 114550 KEGG: hsa:1033 STRING: 9606.ENSP00000335357 UniGene: PMID: 28109073 the mechanism of CDKN3 overexpression in human cancer PMID: 28504190 CDKN3 is frequently upregulated in gastric cancer tissues and cell lines and is related to advanced clinical stage, recurrence, and poor clinical outcome in gastric cancer. The functional data strongly suggest that CDKN3 behaves as an oncogene in gastric cancer, and downregulation of CDKN3 could inhibit gastric cancer cell proliferation, migration, and invasion, and induce cell cycle arrest and apoptosis. PMID: 27983933 CDKN3 may act as a tumor suppressor in liver tissues by modulation of the cell survival signal transduction, monitoring carcinogenesis and elimination of abnormal cells. PMID: 27314282 These results suggest that CDKN3 acts as an oncogene during breast cancer progression. The in vitro silencing of CDKN3 promoted apoptosis, induced G1 phase cell cycle arrest and inhibited cell migration. PMID: 27314680 Knockdown of Cdkn3 stabilizes Mps1 at centrosomes. PMID: 26586430 CDKN3 mRNA may be a good survival biomarker and potential therapeutic target in cervical cancer PMID: 26372210 CDKN3 overexpression in lung adenocarcinoma is not attributed to alternative splicing or mutation but is likely due to increased mitotic activity, arguing against CDKN3 as a tumour suppressor PMID: 26554648 CDKN3 knockdown reduces cell proliferation, invasion and promotes apoptosis in human ovarian cancer cells. PMID: 26191143 These results highlight the importance of CDKN3 in Bcr-Abl-mediated leukemogenesis. PMID: 25360622 High CDKN3 expression is associated with colorectal cancer. PMID: 25735390 these data identify KAP as a major regulator of cell division via interactions with numerous target proteins. aberrant splicing or miR-26a decreases KAP expression to promote glioblastoma growth and invasion. PMID: 24704824 CDKN3 may play an important role in the development and proliferation of epithelial ovarian cancer PMID: 24573179 KAP is overexpressed in alcohol-related hepatocellular carcinoma. PMID: 23292002 RelB activation is key for promoting multiple myeloma cell survival through the upregulation of anti-apoptotic proteins, in particular, CIAP2. PMID: 23555623 CDKN3 controls mitosis through the CDC2 signaling axis. PMID: 23775190 High CDKN3 expression is associated with cervical cancer. PMID: 23405241 cyclin-dependent kinase-associated protein phosphatase expression was associated with poorly differentiated Renal cell carcinoma PMID: 21396835 These results suggest that CDKN3 acts as an oncogene in human hepatocellular carcinoma and antagonism of CDKN3 may be of interest for the treatment of HCC. PMID: 22390936 analysis of CDKN3 cell cycle networks and the molecular mechanism of non-malignancy associated hepatitis/cirrhosis and HCC transformation PMID: 21535270 Identification of a KAP domain that interacts with cyclin-dependent kinase 2. PMID: 12745075 In choline-deficient neuroblastoma cells, the promoter of the cyclin-dependent kinase inhibitor 3 gene (CDKN3) was hypomethylated. This was associated with increased expression of CDKN3 gene product kinase-associated phosphatase (KAP) PMID: 15147518 Pax3 represses transcription through a novel mechanism involving competition between corepressor KAP1 and the heterochromatin-binding protein HP1gamma PMID: 16945326 the reduction of KAP1 levels promotes p53-dependent p21 induction and inhibits cell proliferation in actinomycin D-treated cells. PMID: 17056014

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.