Recombinant Human 2-5A-Dependent Ribonuclease (RNASEL) Protein (GST)

Name: Recombinant Human 2-5A-Dependent Ribonuclease (RNASEL) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-01188P
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 2-5A-Dependent Ribonuclease (RNASEL) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q05823
Target Symbol	RNASEL
Synonyms	(2-5A-dependent RNase)(Ribonuclease 4)(Ribonuclease L)(RNase L)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC
Expression Range	1-741aa
Protein Length	Full Length
Mol. Weight	111.0 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	Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover. Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.
Subcellular Location	Cytoplasm. Mitochondrion.
Protein Families	Protein kinase superfamily
Database References	HGNC: 10050 OMIM: 176807 KEGG: hsa:6041 STRING: 9606.ENSP00000356530 UniGene: PMID: 28418037 Our study suggests that RNASEL:p.Glu265* may be a genetic modifier of risk for early-onset breast cancer predisposition in carriers of high-risk mutations. PMID: 29422015 Results reported in the present study suggest a sex-specific interaction between miR-146a and RNASEL genes in melanoma skin cancer susceptibility. PMID: 28654546 These results demonstrate that ablation of RNase L activity promotes survival of ADAR1 deficient cells even in the presence of MDA5 and MAVS, suggesting that the RNase L system is the primary sensor pathway for endogenous dsRNA that leads to cell death. PMID: 28362255 Mutations in the genes glucokinase regulatory protein (GCKR), RNase L (RNASEL), leukocyte immunoglobulin-like receptor 3 (LILRA3), and dynein axonemal heavy chain 10 (DNAH10) segregated with elevated HDLc levels in families, while no mutations associated with low HDLc. PMID: 24891332 findings suggest that beside the RLR pathway, RNase L cleavage products can also activate the NLRP3-inflammasome pathway, which requires DHX33 (DExD/H-box helicase) and the mitochondrial adaptor protein MAVS. PMID: 26987611 This study provides the evidence that germline variations in RNASEL are associated with fatal PCa in men (Gleason score >7 for rs486907 and RNASEL underexpressed [P = 0.007] in patients with PCa). PMID: 27318894 By sequencing abundant RNA fragments generated by RNase L in cell lines, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation. PMID: 28808124 RNASEL rs3738579 genotype was significantly related to severe necroinflammatory activity (NIA) grade of chronic hepatitis C patients. PMID: 28704535 Serum RNase-L levels were inversely associated with metabolic syndrome and age. PMID: 28399925 We show that mutations in RNase L found in HPC patients may promote prostate cancer by increasing expression of AR-responsive genes and cell motility and identify novel roles of RNase L as a prostate cancer susceptibility gene. PMID: 28257035 Suggest that naturally occurring mutations in the RNase L gene might promote enhanced prostate cancer cell migration and metastasis. PMID: 26517238 This review outlines the role of RNase-L in antimicrobial immunity and the cytoskeleton-associated innate response. [review] PMID: 26760998 Data show that RNA decay by ribonuclease L (RNase L) has an important role in homeostasis and serves as a suppressor of cell adhesion. PMID: 26668391 Single Nucleotide Polymorphisms in RNASEL involved in the immune response are generally not associated with intraprostatic inflammation in men without a Prostate cancer diagnosis. PMID: 26771888 OAS3 displayed a higher affinity for dsRNA in intact cells than either OAS1 or OAS2, consistent with its dominant role in RNase L activation. PMID: 26858407 Tanslation of vaccinia virus A27L and B5R genes is independent of PKR activation, but their expression is dependent on the RNase L activity. PMID: 26656695 Our results demonstrate a novel role of RNase L generated small RNAs in cross-talk between autophagy and apoptosis that impacts the fate of cells during viral infections and cancer. PMID: 26263979 Among 794 RNASEL Ssingle nucleotide polymorphism (SNPs) entries 124 SNPs were found nonsynonymous (ns) from which SIFT predicted 13 nsSNPs as nontolerable whereas PolyPhen-2 predicted 28. PMID: 26236721 Virus infection and RNase L activation disrupt its association with Filamin A and release RNase L to mediate its canonical nuclease-dependent antiviral activities. PMID: 25352621 These data show that RNase L targets specific sites in both host and viral RNAs to restrict influenza virus replication when NS1 protein is disabled. PMID: 25540362 The IFNs inhibit viral infections in part through the 2',5'-oligoadenylate (2-5A) synthetase (OAS)/RNase L pathway. PMID: 24905202 a model of feedback regulation in which RNase L and TTP target SRF mRNA and SRF-induced transcripts. PMID: 25301952 data suggest that RNASEL, an enzyme involved in RNA turnover, is controlled by miR-146a and may be important in NMSC etiology PMID: 24699816 The combined high affinity for double-stranded RNA and the capability to produce 2'-5'-linked oligoadenylates of sufficient length to activate RNase L suggests that OAS3 is a potent activator of RNase L. PMID: 25275129 This study identified three RNASEL variants that are associated with risk for prostate cancer. PMID: 21360564 RNAse L gene SNP 1385G>A does not have a clear clinical significance in CHC. PMID: 25286525 RNase L activity limits FFA/obesity-induced impairment of insulin response in muscle cells via TLR3 and MnSOD expression. PMID: 24651439 This work identifies novel roles for IFN-beta and RNase L in cell barrier functions that are targeted by bacterial effectors to escape host defense mechanisms and promote virulence. PMID: 24733098 Association between SNPs from RNASEL and chromosome 8q24 with the risk of prostate cancer, and its aggressiveness, in a Hispanic (Chilean) population. PMID: 24224612 this study reports 2.8 and 2.1 angstrom crystal structures of human RNase L in complexes with synthetic and natural ligands and a fragment of an RNA substrate. PMID: 24578532 We show an association between RNASEL SNP rs12757998 and outcome after radiation therapy for prostate cancer PMID: 23382116 the structural changes of human RNase L as a result of interactions with four different activators: natural 2-5 pA(4) and three tetramers with 3'-end AMP PMID: 22691533 Data show that miR-29 acts via 4 target sites within the RNASEL 3' UTR. PMID: 23113544 RNASEL mutations are associated with xenotropic murine leukemia virus and its R426Q polymorphism in patients with prostate cancer PMID: 23098452 Two molecules of 2-5A at a time tether RNase L monomers via the ankyrin-repeat (ANK) domain. Each ANK domain harbors two distinct sites for 2-5A recognition that reside 50 A apart. PMID: 23084743 among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase L-dependent antiviral activity against HCV PMID: 23196181 RNase L induces autophagy via c-Jun N-terminal kinase and double-stranded RNA-dependent protein kinase signaling pathways. PMID: 23109342 study found that RNase L is highly expressed in lung cancer cells with significantly decreased enzymatic activity due to an increase of RLI, a specific inhibitor of RNase L PMID: 22925698 Positive selection has operated on the RNASEL gene. PMID: 22513284 Statistically significant differences were found between controls and patients in some of the genotyped regions of the RNASEL gene PMID: 22464196 genotypes associated with the worst prognoses in prostate cancer are G/G in D541E, A/A in R462Q and A/G in I97L. PMID: 22083266 The RNASEL 541Gln allele might be a low-penetrent risk factor for sporadic prostate cancer. PMID: 21656378 Five SNPs were validated as being significantly associated with prostate cancer mortality, one each in the LEPR, CRY1, RNASEL, IL4, and ARVCF genes. PMID: 21846818 The RNASEL -1385G/A polymorphism is associated with cancer risk in African descendents. PMID: 21221811 Ribonuclease L (RNASEL) protein was shown to be up-regulated in lopinavir-treated SiHa cells, which was confirmed by PCR and western blot. Targeted silencing of RNASEL reduced the sensitivity of SiHa cells to lopinavir. PMID: 21685539 Codon 462 polymorphisms within the RNASEL gene are not associated with an increased risk of cervical cancer. PMID: 21665181 Data show that the IQ motif-containing Ras GTPase-activating-like protein 1 (IQGAP1) can associate with RNase L, and that phosphorylation occurs on the IQGAP1, and works as a regulator in apoptosis. PMID: 20875083 Genetic variation is associated with RNASEL associated with prostate cancer. PMID: 20576793 These studies suggest that the expression of Xpr1 and certain genotypes of the RNASEL gene, which could restrict XMRV infection, may play important roles in defining XMRV tropisms in certain cell types. PMID: 20410264

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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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