Recombinant Human Atp-Dependent Rna Helicase Ddx1 (DDX1) Protein (His&Myc)

Name: Recombinant Human Atp-Dependent Rna Helicase Ddx1 (DDX1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00565P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Atp-Dependent Rna Helicase Ddx1 (DDX1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q92499
Target Symbol	DDX1
Synonyms	(DEAD box protein 1)(DEAD box protein retinoblastoma)(DBP-RB)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
Expression Range	1-740aa
Protein Length	Full Length
Mol. Weight	89.9 kDa
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	Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA.; (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs.; (Microbial infection) Required for Coronavirus IBV replication.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasmic granule. Cytoplasm, cytosol. Mitochondrion.; Cytoplasm.
Protein Families	DEAD box helicase family, DDX1 subfamily
Database References	HGNC: 2734 OMIM: 601257 KEGG: hsa:1653 STRING: 9606.ENSP00000233084 UniGene: PMID: 29679569 LGR5 is a critical effector of DDX1 in colorectal cancer cells. PMID: 29869821 data have demonstrated that Venezuelan equine encephalitis virus (VEEV)-nsP3 associates with DDX1 and DDX3 in infected cells to facilitate viral multiplication; determined that VEEV-nsP3 interacts with a pre-formed translational complex, comprising of DX3:eIF4A:eIF4G:PABP to potentially aid in translation of viral proteins. PMID: 27105836 the two structural homologs FAM98A and FAM98B included in a novel complex with DDX1 and C14orf166 are required for PRMT1 expression in colorectal cancer cell lines PMID: 28040436 DDX1 binds HIV-1 rev response element to promote virus assembly. PMID: 28379444 DDX1, a RNA helicase also implicated in DSB repair, interacts with RIF1. Recruitment of DDX1 to DSBs is dependent on RIF1. DDX1 is also required for chromatin loading of BLM to ionizing radiation-induced DSBs. DDX1 and RIF1 have different nucleic acid requirements for accumulation at DSBs, with RNA-DNA hybrids required for DDX1 accrual at DSBs, and single-strand RNA required for accumulation of RIF1 at these sites. PMID: 28544931 Data provide evidence for a role for DDX1 in resolving RNA-DNA structures that accumulate at DNA double-strand breaks located at sites of active transcription thereby facilitating repair by homologous recombination. PMID: 27550810 crystal structure of the SPRY domain of human DDX1 (hDSPRY) is reported at 2.0 A resolution PMID: 26323305 HIV-1 wild type Tat co-immunoprecipitated with DDX1. PMID: 25496916 Data indicate a tight binding of DEAD-box protein DDX1 to adenosine diphosphate (ADP), one of the strongest affinities observed for DEAD-box helicases. PMID: 25690890 hCLE/C14orf166 associates with DDX1, HSPC117, and FAM98B in a novel transcription-dependent shuttling RNA-transporting complex. PMID: 24608264 archease (also called ZBTB8OS), a protein of unknown function, is required for full activity of the human tRNA ligase complex and, in cooperation with DDX1, facilitates the formation of an RTCB-guanylate intermediate central to mammalian RNA ligation PMID: 24870230 subcellular localization of KSRP is regulated by competing interactions with DDX1 or 14-3-3 PMID: 24023901 DDX1 depletion causes accumulation of DNA damage in response to cisplatin and defects in DNA repair of double-stranded breaks. PMID: 23797032 DDX1 was shown to be an RNA-activated ATPase, wherein Rev-bound RNA was equally effective at stimulating ATPase activity as protein-free RNA. PMID: 22051512 DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element. PMID: 21763499 elevated levels of DDX1 RNA or the presence of DDX1 in the cytoplasm could serve as an effective prognostic biomarker for early recurrence in primary breast cancer. PMID: 20499159 DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication. PMID: 20573827 determination as a homopolymeric poly(A) RNA-binding protein PMID: 12183465 These findings indicate that DDX1 is a critical cellular co-factor for Rev function, which maintains the proper subcellular distribution of this lentiviral regulatory protein. PMID: 15567440 DEAD box proteins and other RNA-binding proteins may play roles in active HIV replication and in the control of viral latency. PMID: 15588285 There may be a subset of NB in which enhanced DDX1 and low-NAG expression consequent to DDX1 co-amplification without NAG amplification contributes to susceptibility to intensive therapy. PMID: 17028906 Biotinylated DNA affinity precipitation and chromatin immunoprecipitation assays confirmed that DDX1 binds specifically to JCV-TCR. PMID: 17380053 DDX1 regulates proliferation of JCV in vitro through transcriptional activation. PMID: 17380054 Concomitant DDX1 and MYCN gain is associated with neuroblastoma PMID: 17611020 DDX1 plays an RNA clearance role at DNA double-strand breaks sites, thereby facilitating the template-guided repair of transcriptionally active regions of the genome. PMID: 18710941 DDX1 mRNA was produced in both seminoma and nonseminoma types of human testicular germ cell tumor samples PMID: 19398953

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.