Recombinant Human Protein Dek (DEK) Protein (His&Myc)

Name: Recombinant Human Protein Dek (DEK) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01406P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein Dek (DEK) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P35659
Target Symbol	DEK
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	SASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS
Expression Range	2-375aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.4 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in chromatin organization.
Subcellular Location	Nucleus. Note=Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.
Database References	HGNC: 2768 OMIM: 125264 KEGG: hsa:7913 STRING: 9606.ENSP00000380414 UniGene: Hs.484813
Associated Diseases	A chromosomal aberration involving DEK is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia (PubMed:1549122). Translocation t(6;9)(p23;q34) with NUP214/CAN (PubMed:1549122). It results in the formation of a DEK-NUP214 fusion gene (PubMed:1549122).
Tissue Specificity	Ubiquitous. Expressed at relatively high levels.

Gene Functions References

These findings define DEK as an important and multifunctional mediator of homologous recombination. PMID: 28317934
DEK is detected in spontaneously forming neutrophil extracellular traps (NETs) from juvenile idiopathic arthritis patient synovial neutrophils, and DEK-targeted aptamers reduce NETs formation. PMID: 28165452
High DEK proto-oncogene protein (DEK) expression associated with complete response to neoadjuvant chemoradiotherapy. PMID: 29409457
High DEK expression is associated with cervical cancer tumorigenesis and metastasis. PMID: 28627610
The results of the present study demonstrated that EMT of colorectal carcinoma cells was partially mediated by DEK, which likely affected the invasive ability of colorectal carcinoma cells. In addition, cell proliferation and apoptosis were susceptible to DEK silencing. PMID: 29115492
RNA-sequencing proved to be a valuable tool for the detection of a fusion of genes DEK and NUP214 in a leukemia that showed cryptic cytogenetic rearrangement of chromosome band 9q34. PMID: 29109093
DEK overexpression enhanced carcinogenesis, including field cancerization, in OSCC by stimulating the G1 /S phase transition and promoting DNA replication. PMID: 28834425
DEK and LCMR1 were demonstrated to cooperate in the inhibition of apoptosis in lung cancer cells. PMID: 28765911
High DEK expression is associated with breast cancer angiogenesis . PMID: 26988756
our study indicates that DEK expression is required for tumorigenesis and metastasis of hepatocellular carcinoma PMID: 27057626
High DEK expression is associated with melanoma progression. PMID: 27893188
DEK correlates with IL6 expression in HPV16+/p16+ oropharyngeal squamous cell carcinomas (OPSCC). PMID: 28423581
data support a scenario whereby overexpression of the human DEK oncogene reprograms keratinocyte metabolism to fulfill energy and macromolecule demands required to enable and sustain cancer cell growth PMID: 28558019
Decreased DEK expression in plasma cells suggests a potential role of this gene in plasma cell development and lack of detectable DEK protein by IHC could be used as a biomarker for normal and malignant plasma cells PMID: 28558048
Our data indicated DEK plays multiple roles to facilitate tumor growth and maintenance. It can be used as a potential target for astrocytic tumor diagnosis and gene therapy. PMID: 28670979
High DEK expression is associated with pancreatic ductal adenocarcinoma. PMID: 27959420
AP-2a is an important transcription factor of DEK expression, which is correlated with the methylation level of the DEK core promoter in hepatocellular carcinoma . PMID: 27499261
miR-592 targets DEK transcript and suppresses hepatocellular carcinoma cell growth PMID: 26722432
Results find that DEK binds to transcription start sites with a dual role in activation and repression of highly and ubiquitously expressed genes. PMID: 25216995
The study identified the DEK oncoprotein as a critical factor that interacts with an essential upstream enhancer element of the EKLF promoter and exerts a positive effect on EKLF levels. PMID: 26303528
DEK promotes the growth of colorectal cancer and apoptosis PMID: 25340858
Data show that oncoprotein DEK facilitates cellular proliferation under conditions of DNA replication stress by promoting replication fork progression. PMID: 25347734
The results show that several leukemia-associated fusion genes cause an increase in DEK protein expression. PMID: 25524609
DEK expression during normal hematopoiesis did reveal a relationship with specific cell types implicating a distinct function during myeloid differentiation PMID: 25128083
These data suggest DEK overexpression as a crucial event for the emergence of an aggressive phenotype in colorectal cancer. PMID: 25515240
Studies demonstrate that DEK overexpression, due in part to Ron receptor activation, drives breast cancer progression through the induction of Wnt/beta-catenin signaling. PMID: 24954505
DEK plays an important role in the progression of small cell lung cancer PMID: 25197373
Results highlight a novel function of DEK as a guardian of chromatin by restricting widespread histone access, and in particular by modulating differential H3.3 loading in specific chromatin areas. PMID: 25049225
t(6;9)/DEK-NUP214 represents a unique subtype of acute myeloid leukemia with a high risk of relapse. PMID: 24441146
data demonstrate that DEK stimulates HNSCC cellular growth and identify DeltaNp63 as a novel DEK effector PMID: 24608431
DEK is an hTERT repressor shared by various leukemia subtypes that may be involved in the deregulation of numerous genes associated with leukemogenesis PMID: 24563617
High level of DEK protein expression predicts the poor prognosis of patients with gastric cancer PMID: 24650035
the expression of the fusion gene DEK-NUP214 leads to increased cellular proliferation. We show that this is dependent on upregulation of the signal transduction protein mTOR with subsequent effects on protein synthesis and glucose metabolism. PMID: 24073922
DEK plays an important role in the progression of colorectal cancers and it is an independent poor prognostic factor of colorectal cancers PMID: 23902796
DEK depletion inhibited cellular migration in lung cancer cell lines possibly through inactivation of the RhoA/ROCK/MLC signal transduction pathway PMID: 23571382
Full-length DEK secreted by one cell can be taken up by another cell, move to the nucleus, and function in heterochromatin biology and DNA repair, thereby potentially uniting the intracellular and extracellular activities of DEK. PMID: 23569252
increased expression of DEK in chronic lymphocytic leukemia correlates with immunoglobulin heavy chain variable gene mutational status, CD38-positive and del(17p13), and DEK can therefore be considered as potential prognostic factor. PMID: 23052131
DEK promotes the pathogenesis of estrogen receptor positive breast cancer. PMID: 23071688
DEK may be involved in the pathogenesis of Merkel cell carcinoma and therefore may provide therapeutic implications for Merkel cell carcinomas. PMID: 22765016
DEK has potent effects on HSCs, HPCs, and hematopoiesis, information of biological and potential clinical interest. PMID: 21943234
C/EBPalpha and DEK coordinately activate myeloid gene expression. PMID: 22474248
DEK knockdown results in a significant growth repression of CaSki cells by inducing cell apoptosis and senescence via upregulation of p65. PMID: 22390170
DEK overexpression appears to be associated with breast cancer progression PMID: 22360505
DEK is important for DNA double-strand break repair. PMID: 21653549
DEK protein is expressed in bladder tumor tissue and voided urine of bladder cancer patients. PMID: 21663673
DEK overexpression may be a frequent event in invasive melanomas, and further augmentation of DEK expression may be associated with the acquisition of ominous features such as deep dermal invasion and metastasis. PMID: 21316078
data indicate that DEK expression stimulates the growth, stem cell character and motility of breast cancer cells, and that DEK-dependent cellular invasion occurs at least in part via beta-catenin activation PMID: 21317931
identify the oncoprotein DEK, an abundant nuclear protein with a previously enigmatic in vivo function, as a Suppressor of Variegation [Su(var)] that is crucial to global heterochromatin integrity PMID: 21460035
DEK can contribute directly to joint inflammation in juvenile idiopathic arthritis by generating ICs through high-affinity interaction between DEK and DEK autoantibodies. PMID: 21280010
DEK overexpression, partly through an increase in its gene dose, mediates the activity of global transcriptional regulators and is associated with tumor initiation activity and poor prognosis in high grade neuroendocrine carcinoma of the lung. PMID: 20543864

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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.