Recombinant Mouse Dna-Dependent Protein Kinase Catalytic Subunit (PRKDC) Protein (His)

Name: Recombinant Mouse Dna-Dependent Protein Kinase Catalytic Subunit (PRKDC) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10082P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Dna-Dependent Protein Kinase Catalytic Subunit (PRKDC) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P97313
Target Symbol	PRKDC
Synonyms	Prkdc; Xrcc7; DNA-dependent protein kinase catalytic subunit; DNA-PK catalytic subunit; DNA-PKcs; EC 2.7.11.1; p460
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	EYPFLVKGGEDLRQDQRIEQIFEVMNAILSQDAACSQRNMQLRTYRVVPMTSRLGLIEWIENTMTLKDLLLSNMSQEEKVANNSDPKAPIRDYKDWLMKVSGKSDAGAYVLMYSRANRTETVVAFRRRESQVPPDLLKRAFVKMSTSPEAFLALRSHFASSHALLCISHWLLGIGDRHLNNFMVAMETGSVIGIDFGHAFGSATQFLPVPELMPFRLTRQFVSLMLPMKETGLMCTVMVHALRAFRSCAGLLTDTMEIFVKEPSFDWKS
Expression Range	3747-4015aa
Protein Length	Partial
Mol. Weight	34.6kDa
Research Area	Others
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	Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ. Act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome. Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Subcellular Location	Nucleus. Nucleus, nucleolus.
Protein Families	PI3/PI4-kinase family
Database References	KEGG: mmu:19090 STRING: 10090.ENSMUSP00000023352 UniGene: Mm.71
Associated Diseases	Defects in Prkdc are the cause of severe combined immune deficiency (SCID) which is characterized by a lack of mature functional lymphocytes and a high susceptibility to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency syndrome in human infants.

Gene Functions References

findings identify a kinase-dependent role of DNA-PKcs in suppressing MH-mediated end joining and a structural role of DNA-PKcs protein in the orientation of class switch recombination. PMID: 30072430
Loss of DNA-PKc expression is associated with impairment of non-homologous end-joining of radiation-induced double strand break repair in nasopharyngeal carcinoma. PMID: 29344644
DNA repair, mediated by DNA-PK, and cell cycle arrest, mediated by p53, cooperate to protect the stem cell niche after DNA damage. PMID: 28686579
Decreasing DNA-dependent protein kinase activity increases AMPK activity and prevents weight gain, decline of mitochondrial function, and decline of physical fitness in middle-aged mice and protects against type 2 diabetes. PMID: 28467930
Ku70 is epistatic with XLF and DNA-PKcs and support a model in which inactivation of Ku70 allows DNA lesions to become accessible to alternative DNA repair pathways (other than Classical Non-Homologous End-Joining (C-NHEJ)). PMID: 28759779
DNA-PKcs deficiency caused inefficient DSB repair at later time points post-IR in both conditions. These observations suggest that DNA-PKcs contributes to the fast and slow repair of DSBs by NHEJ. PMID: 27136939
The SAGA deubiquitinase activity was required for optimal irradiation-induced gammaH2AX formation, and failure to remove H2BK120ub inhibits ATM- and DNAPK-induced gammaH2AX formation. PMID: 27160905
functional DNA-PKcs T2609 cluster is required to facilitate telomere leading strand maturation and prevention of genomic instability and cancer development. PMID: 26616856
TMU-35435 enhances etoposide cytotoxicity by regulating ubiquitin-proteasomal degradation of DNA-PKcs and inhibiting the DNA repair pathway in triple negative breast cancer cells. PMID: 28450160
DNA-PKcs are required to prevent endogenous DNA damage accumulation throughout the adult brain. PMID: 28123024
DNA-PK inhibition and siRNA-mediated DNA-PK knockdown blocked cell fusion in myoblasts which implicate a new role for DNA-PK in myogenic differentiation. PMID: 27513301
protein deficiency impairs Ig class switch recombination PMID: 26546606
AIM2 reduced Akt activation and tumor burden in colorectal cancer models, while an Akt inhibitor reduced tumor load in Aim2(-/-) mice PMID: 26107252
PRKDC proteins that mediate non-homologous end joining have been identified as TRIP13 binding partners in head and neck cancer. PMID: 25078033
NR5A1 prevents centriole splitting by inhibiting centrosomal DNA-PK activation and beta-catenin accumulation PMID: 25421435
Results show that DNA-PKcs functions as a selective modulator of transcriptional networks that induce cell migration, invasion, and metastasis of prostate cancer cells. PMID: 26175416
These experiments define a novel requirement for 53BP1 in the fusions of DNA-PKcs-deficient telomeres throughout the cell cycle. PMID: 25264618
data suggest that DNA-PKcs-SIN1 complexation-mediated Akt activation (Ser-473 phosphorylation) is required for mouse osteoblast differentiation PMID: 25264192
Activated platelets accumulate in the brain rescue apoptotic neuron cells via activation of EGFR and DNA-dependent protein kinase. PMID: 25210793
DNA-PK and ATM acts in parallel upstream of XRCC4, regulating through phosphorylation PMID: 25391321
DNA-PKcs is the molecular switch that coordinates end-processing and end-ligation at the DNAends through differential phosphorylations. PMID: 25818648
DNA-PK/Chk2 signaling induces centrosome amplification upon long-term HU treatment, therefore increasing our insight into tumor recurrence after initial chemotherapy. PMID: 24662822
DNA-PK is a DNA sensor for IRF-3-dependent innate immunity. PMID: 23251783
A novel regulatory pathway where signaling from DNA-PK appears to suppress midbrain-specific Lmx1a expression. PMID: 24194952
Inactivation of Ku80 and DNA-PKCS causes reduced lifespan and bodyweight. PMID: 24740260
Thus SB and PB transposons represent a promising non-viral approach for iPS cell derivation. PMID: 24928388
GANP plays a positive role in IgV region diversification of DT40 B cells in a nonhomologous end joining-proficient state. DNA-PKcs physically interacts with GANP, and this interaction is dissociated by dsDNA breaks PMID: 24808370
IP7, formed by IP6K2, binds CK2 to enhance its phosphorylation of the Tti1/Tel2 complex, thereby stabilizing DNA-PKcs and ATM. This process stimulates p53 phosphorylation at serine 15 to activate the cell death program. PMID: 24657168
the inhibition of DNA-PK-dependent DNA sensing by a poxvirus protein, adding to the evidence that DNA-PK is a critical component of innate immunity to DNA viruses. PMID: 24098118
interaction between DNA-PKcs and Snail1 might be an effective strategy for sensitizing cancer cells and inhibiting tumor migration PMID: 24085291
During V(D)J recombination, DNA-PKcs repairs coding DNA ends. DNA-PKcs deficiency leads to a nearly complete block in coding join formation, as DNA-PKcs is required to activate the endonuclease that opens hairpin-sealed coding ends. PMID: 23836881
XLF functionally overlaps with DNA-PKcs in normal development, promotion of genomic stability in fibroblasts, and in IgH class switch recombination in mature B cells. PMID: 23345432
DNA-PK is needed to generate the phosphorylated form of H2AX that controls necroptosis. PMID: 22972376
our results suggest that DNA-PKcs may interact with Aire to promote the expression of Toll-like receptors in RAW264.7 cells. PMID: 22239103
Lack of DNA-PKcs is accompanied by an increase in the protein level of one of the catalytic isozymes of protein kinase CK2, i.e., CK2alpha' and a concomitant increase in CK2 activity. PMID: 21750982
RAD50, DNA-PKcs kinase activity, and transcription context are each important to limit incorrect end use during EJ repair of multiple DSBs, but each has distinct roles during repair events requiring end processing PMID: 22027841
We concluded that phosphorylation of DNA-activated protein kinase catalystic subunit is essential for the normal activation of multiple DNA repair pathways, which in turn is critical for the maintenance of diverse populations of tissue stem cells in mice. PMID: 21482716
Our results demonstrate that both Prkdc SNPs are responsible for deficient DNA-PKcs protein expression, DNA repair and telomere function, while the LEWES SNP affects only DNA-PKcs expression and repair capacity. PMID: 21265624
DNA-PK is implicated in the repair of double-stranded DNA breaks during neurogenesis in the developing retina PMID: 20448641
treatment of DNA-PKcs- or ATM-deficient cells, respectively, with specific kinase inhibitors for ATM or DNA-PKcs recapitulates SJ defects, indicating that overlapping V(D)J recombination functions of ATM and DNA-PKcs are mediated through kinase activities PMID: 21245310
Atm and DNA-PKcs have overlapping catalytic activities that are required for chromosomal signal joint formation and for preventing the aberrant resolution of signal ends as potentially oncogenic chromosomal translocations PMID: 21245316
Data implicate mtDNA damage in the development of adriamycin toxicity and identify Prkdc as a mtDNA depletion syndrome modifier gene and a component of the mitochondrial genome maintenance pathway. PMID: 20978358
MiR-101 could efficiently target DNA-PKcs and ATM via binding to the 3'- UTR of DNA-PKcs or ATM mRNA. PMID: 20617180
the nucleotide sequence of approximately 193-kbp and 84-kbp genomic regions encoding the entire Prkdc gene PMID: 11839092
required for p53-dependent apoptosis in mouse embryo fibroblasts PMID: 12065413
DNA-PK role in radioadaptive response of mouse spleen PMID: 12194752
Generating mice doubly deficient in DNA-PKcs and telomerase (Terc(-/-)/DNA-PKcs(-/-))shows that DNA-PKcs also has a fundamental role in telomere length maintenance, suggesting suggest a critical role of DNA-PKcs in both cancer and aging. PMID: 12426399
The function of DNA-dependent protein kinase catalytic subunit is retained in DNA-PKcs-deficient dendritic cells (DC) from knockout mice, therefore DNA-PKcs is not essential for DC responses to CpG DNA. PMID: 12626561
Evidence is found that chromosome 16 segments from BALB/c that encode Prkdc interact with Apc(Min) (multiple intestinal neoplasia) and specifically enhance IR-induced adenoma development in the upper part of the small intestine. PMID: 12750251
BALB/c alleles for Prkdc and Cdkn2a interact to modify mammary tumor susceptibility in Trp53+/- mice. PMID: 12750252

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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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