Recombinant Human Risc-Loading Complex Subunit Tarbp2 (TARBP2) Protein (GST)

Name: Recombinant Human Risc-Loading Complex Subunit Tarbp2 (TARBP2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08867P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Risc-Loading Complex Subunit Tarbp2 (TARBP2) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q15633
Target Symbol	TARBP2
Synonyms	LOQS; Prbp; RISC loading complex subunit TARBP2; RISC-loading complex subunit tarbp2; TAR (HIV 1) RNA binding protein 2; TAR (HIV) RNA binding protein 2; TAR (HIV) RNA-binding protein TRBP1; TAR RNA Binding Protein 2; TAR RNA-binding protein 2; tarbp2; TARBP2 RISC loading complex RNA binding subunit; Trans-activation-responsive RNA-binding protein; TRBP; TRBP1; TRBP2; TRBP2_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPVFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEVEPDDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCRVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCHGSATTREAARGEAARRALQYLKIMAGSK
Expression Range	1-366aa
Protein Length	Full Length
Mol. Weight	66.0kDa
Research Area	Microbiology
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 formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1.; (Microbial infection) Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs. This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR. Mediates recruitment of FTSJ3 methyltransferase to HIV-1 RNA, leading to 2'-O-methylation of the viral genome, allowing HIV-1 to escape the innate immune system.
Subcellular Location	Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
Protein Families	TARBP2 family
Database References	HGNC: 11569 OMIM: 605053 KEGG: hsa:6895 STRING: 9606.ENSP00000266987 UniGene: PMID: 29348664 A statistically significant association with the risk of AD was observed with the CT genotype for rs784567 on the TARBP2 gene. on controlling for age and sex, we found that for the TARBP2-RNASEN association with AD the age variation was a risk factor for AD risk (P<0.001; OR=1.104; 95% CI, 1.059-1.151). PMID: 26796812 TRBP is a novel transcriptional coactivator of the Notch signaling pathway, playing an important role in neural stem cell regulation during mammalian brain development PMID: 28174252 TRBP is required for normal antiviral responses to Cardiovirus infection. PMID: 27743889 Experimental and computational techniques were employed to examine the hypothesis that TRBP-double-stranded RNA-binding domain (dsRBD) 2 binding by a 20-mer dsRNA is coupled with RNA bending, results suggest that this particular dsRBD-dsRNA interaction produces little to no change in the A-form geometry of dsRNA in solution PMID: 27332119 We propose that the S6K2/TRBP node controls miRNA biogenesis in HDLECs and provides a molecular link between the mTOR pathway and the miRNA biogenesis machinery. PMID: 27407113 TARBP2 silencing inhibits in vitro invasion and migration of NCIH1299 nonsmall cell lung cancer cell via the JNK/STAT3/AKT pathway. TARBP2 silencing does not significantly affect cell growth. PMID: 27599909 TARBP2 has roles in tumor development and progression [review] PMID: 26486325 SUMOylation of TARBP2 is required for regulating siRNA efficiency. PMID: 26582366 HIV-1 Rev-response element RNA acts as an RNA silencing suppressor by competing with TRBP-bound siRNAs. PMID: 25668122 the role of TRBP and unveils negative feedback regulation of PKR through TRBP phosphorylation. PMID: 25437560 Results show the crystal structure of the interface between microRNA biogenesis proteins Dicer and TRBP. Mutations in this interface prevent recruitment of TRBP to Dicer. PMID: 25557550 RPL5 binds to the TRBP2 and Ago2 subunits of the RISC and mediates the binding to c-Myc 3'UTR. PMID: 24141778 TARBP2 expression is upregulated in late-stage breast cancer and triple-negative breast cancer and may have a role in poorer disease-free survival and overall survival PMID: 24563327 identified TARBP2, a double-stranded RNA-binding protein implicated in microRNA processing, as the trans factor that binds the sRSE family and similar structural elements--collectively termed TARBP2-binding structural elements (TBSEs)--in transcripts PMID: 25043050 Tarbp2 binding to TRPC4 promotes changes of cytosolic Ca(2+) and, thereby, leads to a dynamic regulation of Dicer activity, essentially at low endogenous Dicer concentrations. PMID: 24563462 mRNA expression of TARBP2, but not DICER or DROSHA, is a strong molecular predictor to discriminate between adrenocortical adenomas and carcinomas PMID: 23671264 in vitro binding patterns of human TRBP and PACT to siRNA PMID: 23658827 The results show that PACT and TRBP have distinct effects on Dicer-mediated dsRNA processing. PMID: 23661684 No frameshift mutations in TARBP2 were identified in a study of 4 cases of upper urinary tract urothelial carcinoma with high microsatellite instability status. PMID: 23690119 Results show that the region of TRBP that binds immature miRNAs comprises two independent double-stranded RNA-binding domains connected by a 60-residue flexible linker. PMID: 23435228 RISC proteins PACT, TRBP, and Dicer, together with PKR, are steroid receptor RNA activator-binding nuclear receptor coregulators that are recruited to the promoters of hormone-regulated genes and regulate the expression of downstream target genes. PMID: 23550157 We report an unanticipated dsRNA diffusion behavior of TRBP, which requires two double-stranded RNA binding domains, and its correlation with the role of TRBP in promoting Dicer-induced RNA cleavage. PMID: 23251028 The studies in this review show that TRBP is multifunctional and mediates cross talk between different pathways. Its activities at the molecular level impact the cellular function from normal development to cancer and the response to infections. PMID: 22933564 There was no significant difference in the TARBP2 expression levels between the epithelial skin cancer groups and the healthy controls (P > 0.05). PMID: 22025453 Depletion of Dicer and TRBP, proteins involved in miRNA biogenesis, reduced HCV RNA accumulation, mature duplex miR-122 abundance, and miR-122 directed mRNA translation suppression, suggesting roles in miR-122 processing. PMID: 22999255 TRBP is a key regulator of miRNA processing and targeting in humans. PMID: 23006623 Data suggest that cancer stem cell (CSC) self-renewal and tumor maintenance may depend on deregulation of TARBP2-dependent miRNA expression. PMID: 22698405 AGO2, PACT and TRBP are required for the efficient functioning of Dicer in cells PMID: 22163034 results demonstrate for the first time that stress-induced PACT phosphorylation functions to free PACT from the inhibitory interaction with TRBP and also to enhance its interaction with PKR PMID: 21526770 The structures dsRNA-bdinding domain 1 and dsRNA binding domain 2 solved by x-ray crystallography and NMR spectroscopy respectively. PMID: 21080422 TARBP2 frameshift mutation is associated with hereditary nonpolyposis colorectal cancer. PMID: 20877318 the three-dimensional structure of human Dicer bound to the protein TRBP at approximately 20 A resolution determined by negative-stain electron microscopy (EM) and single-particle analysis PMID: 19836333 binds to merlin, which inhibits its oncogenic activity; results provide the first clue to the functional interaction between TRBP and merlin and suggest a novel mechanism for the tumor suppressor function of merlin both in vitro and in vivo PMID: 15123692 Data suggest that the cell specifity of HIV-1 expression and replication may be regulated, in part, through the control of TRBP1 expression by NF-Y factors. PMID: 16343534 These results suggest that, in the context of HIV replication, TRBP contributes mainly to the enhancement of virus production and that Dicer does not mediate HIV restriction by RNAi. PMID: 17360756 Results indicate that human TRBP and PACT directly interact with each other and associate with Dicer to stimulate the cleavage of double-stranded or short hairpin RNA to siRNA. PMID: 17452327 Ago2, Dicer, and TRBP comprise the RISC-loading complex (RLC) and assembles spontaneously in vitro from purified components PMID: 18178619 TRBP controls PACT activation of PKR, an activity that is reversed by stress. PMID: 18936160 RDE-4 preferentially binds long dsRNA, while TRBP binds siRNA with an affinity that is independent of dsRNA length. PMID: 18948111 The RLC Dicer's N-terminal DExH/D domain, located in a short 'base branch', interacts with TRBP, whereas its C-terminal catalytic domains in the main body are proximal to AGO2. PMID: 19820710

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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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