Recombinant Human Mediator Of Dna Damage Checkpoint Protein 1 (MDC1) Protein (His-SUMO)

Name: Recombinant Human Mediator Of Dna Damage Checkpoint Protein 1 (MDC1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09375P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Mediator Of Dna Damage Checkpoint Protein 1 (MDC1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14676
Target Symbol	MDC1
Synonyms	Homologue to Drosophila photoreceptor protein calphotin; MDC 1; Mdc1; MDC1_HUMAN; Mediation of DNA damage checkpoint 1; Mediator of DNA damage checkpoint 1; Mediator of DNA damage checkpoint protein 1; NFBD 1; NFBD1; Nuclear factor with BRCT domains 1; Nuclear Factor with BRCT Domains Protein 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	APKVLFTGVVDARGERAVLALGGSLAGSAAEASHLVTDRIRRTVKFLCALGRGIPILSLDWLHQSRKAGFFLPPDEYVVTDPEQEKNFGFSLQDALSRARERRLLEGYEIYVTPGVQPPPPQMGEIISCCGGTYLPSMPRSYKPQRVVITCPQDFPHCSIPLRVGLPLLSPEFLLTGVLKQEAKPEAFVLS
Expression Range	1892-2082aa
Protein Length	Partial
Mol. Weight	36.9 kDa
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	Required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1.
Subcellular Location	Nucleus. Chromosome. Note=Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires 'Ser-139' phosphorylation of H2AX. Colocalizes with APTX at sites of DNA double-strand breaks.
Database References	HGNC: 21163 OMIM: 607593 KEGG: hsa:9656 STRING: 9606.ENSP00000365588 UniGene: PMID: 28921460 These findings indicate that the c-Fos/miR-22/MDC1 axis plays a relevant role in DNA repair in terminally differentiated cells, which may facilitate our understanding of molecular mechanism underlying the downregulating DNA repair in differentiated cells. PMID: 28637007 key component of the DNA damage response and interacts with several factors such as gamma-H2AX PMID: 29026069 prognostic marker in predicting relapse-free survival in oral squamous cell carcinoma PMID: 28161894 It showed a link between the status of MDC1 protein and TP53 gene, which specific mutations caused radiation-induced MDC1 down-regulation. PMID: 28397142 ASF1a promotes non-homologous end joining repair by facilitating phosphorylation of MDC1 by ATM at double-strand breaks. PMID: 28943310 the opposing activities of RNF4 and ataxin-3 consolidate robust MDC1-dependent signaling and repair ofDNA double-strand break. PMID: 28275011 NFBD1 protein is overexpressed in NPC tissues and that silencing NFBD1 can inhibit cell growth, induce apoptosis, increase the production of intracellular ROS. NFBD1 knockdown also inhibits the tumorigenicity of NPC cells in vivo. PMID: 28081741 NFBD1 knockdown improves the chemosensitivity of NPC cells by inhibiting cell growth and promoting apoptosis through the impairment of DNA damage repair, suggesting NFBD1 as a novel therapeutic target for NPC. PMID: 27334757 knockdown of MCM2 or MCM6 could significantly inhibit foci forming of MDC1 in TE-1 nuclei in response to bleomycin-induced DNA damage (p < 0.001). This study indicates the direct interaction between MDC1 and MCMs in TE-1 nuclei. PMID: 27908247 MDC1 recruits TNKS1 and TNKS2 to DNA lesions. PMID: 26845027 MDC1 silencing enhances the radiosensitivity of human nasopharyngeal cancer CNE1 cells and results in xenograft tumor growth inhibition. PMID: 26247734 we generated two HEP-2 cell lines with a stable knockdown of MDC1 or 53BP1 with short hairpin RNA (shRNA), respectively, and investigated the effect of MDC1 and 53BP1 on cell radiosensitivity PMID: 25976740 During replicative senescence and stress-induced premature senescence, MDC1 is downregulated by upregulating miR-22. PMID: 25627978 we have identified a novel antisense lncRNA MDC1-AS, which may participate in bladder cancer through up-regulation of its antisense tumor-suppressing gene MDC1 PMID: 25514464 our findings suggest that MDC1 promotes ovarian cancer metastasis through the induction of EMT. PMID: 25592380 The study suggest that MDC1 as an epigenetic modifier regulates androgen receptor transcriptional activity and MDC1 may function as a tumor suppressor of prostate cancer. PMID: 25934801 data suggested that the SNP rs4713354A>C of MDC1 may be a functional genetic biomarker for susceptibility to lung cancer in Chinese PMID: 25198518 NFBD1/MDC1 is phosphorylated by PLK1 and controls G2/M transition through the regulation of a TOPOIIalpha-mediated decatenation checkpoint. PMID: 24349352 ATM and MDC1 maintain genomic stability not only by controlling the DNA damage response, but also by regulating spindle assembly checkpoint activation, providing an important link between these two essential biological processes. PMID: 24509855 The TOPBP1 phosphate-binding pocket and positively charged residues in a variant loop in BRCT5 present an extended binding surface for the negatively charged MDC1 phosphopeptide. PMID: 23891287 Silencing MDC1 can enhance the radiosensitivity of esophageal squamous cell carcinoma ECA109 cells in vitro. PMID: 20813677 PARP1 activation and BAL1-BBAP recruitment to DNA damage sites are independent of ATM and MDC1. PMID: 23230272 proteins accumulate into foci with characteristic mean recruitment times tau(1). Mdc1 accumulates faster than 53BP1 after high LET irradiation PMID: 22860035 inhibition in the activity of the core mitotic regulator CDK1 enhances MDC1-gammaH2AX colocalization in mitosis. PMID: 22962268 A dual interaction between the DNA damage response protein MDC1 and the RAG1 subunit of the V(D)J recombinase. PMID: 22942284 distinct dynamics of MDC1 and 53BP1 at different types of nuclear structures PMID: 22677490 It was shown that MDC1 is sumoylated after DNA damage, and sumoylation of MDC1 at Lys1840 is needed for MDC1 degradation and removal of MDC1 and 53BP1 from DNA damage sites. Sumoylated MDC1 was ubiquitinated by the SUMO-targeted E3 ubiquitin ligase RNF4. PMID: 22635276 A major binding target of the Mdc1 FHA domain is a previously unidentified DNA damage and ATM-dependent phosphorylation site near the N-terminus of Mdc1 itself. PMID: 22234878 expression of NFBD1 seems to be related to the oncogenic potential of cervical cancer, and suppression of its expression can inhibit cancer cell growth both in vitro and in vivo PMID: 21853275 As compared to the MDC1 forkhead-associated FHA) domain, the MU2 FHA domain dimerizes using a different and more stable interface and contains a degenerate phosphothreonine-binding pocket. PMID: 22273583 MDC1 is required for the recruitment of RAP80 to DNA double-strand breaks. PMID: 21857162 structural insight into MDC1-CHK2 interaction PMID: 22211259 This study provides the first evidence that interactions involving MDC1 can be regulated by ubiquitylation PMID: 21622030 most NFBD1 regulated genes are regulated in both the absence and presence of IR, thus pointing toward a novel function for NFBD1 outside of the DNA damage response PMID: 21551225 this study reveals that human NIPBL is a novel protein recruited to DSB sites, and the recruitment is controlled by MDC1, RNF168 and HP1gamma. PMID: 21784059 The specific TopBP1-MDC1 interaction was mediated by the fifth BRCT domain of TopBP1 and the Ser-Asp-Thr repeats of MDC1. TopBP1 accumulation at stalled replication forks was promoted by the H2AX/MDC1 signaling cascade. PMID: 21482717 Mediator of DNA damage checkpoint protein 1 (MDC1) has a role in nodal recurrence in early-stage breast cancer patients treated with breast-conserving surgery and radiation therapy PMID: 20521098 Results implicate MDC1 in the cellular apoptotic response. PMID: 21148072 High NFBD1 is associated with esophageal cancer. PMID: 20364298 The viral oncoprotein tax sequesters DNA damage response factors by tethering MDC1 to chromatin. PMID: 20729195 NFBD1 has a pivotal role in the regulation of proper mitotic entry. PMID: 20529673 MDC1 and 53BP1 expressions were observed for the first time in human esophageal carcinoma cell lines TE-1,TE-13 and Eca109 cells, at both the mRNA and protein levels. PMID: 17884766 structure & peptide binding specificity of BRCT domains of MDC1 & BRCA1; crystal structures of BRCA1 & MDC1 bound to peptides show differences in the environment of conserved arginines that determine affinity for peptides with -COO(-) vs -CO-NH(2) termini PMID: 20159462 This nuclear protein with signature motifs of FHA and BRCT, and an internal 41-amino acid repeat sequence, is an early participant in DNA damage response. PMID: 12475977 role in DNA damage signaling pathways PMID: 12499369 NFBD1 is parallel to 53BP1 in regulating Chk2 and downstream of H2AX in the recruitment of repair and signaling proteins to sites of DNA damage in tumor cells PMID: 12551934 MDC1-mediated focus formation by the MRE11 complex at sites of DNA damage is crucial for the efficient activation of the intra-S-phase checkpoint PMID: 12607003 MDC1 is recruited through its FHA domain to the activated CHK2 and has a critical role in CHK2-mediated DNA damage responses PMID: 12607004 role for MDC1 in mediating transduction of the DNA damage signal PMID: 12607005

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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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