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AB181920

重组人 TRBP 蛋白 (denatured) (Tag Free)

Recombinant Human TRBP protein (denatured) (Tag Free)

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(1 Publication)

Recombinant Human TRBP protein (denatured) (Tag Free) is a Human Full Length protein, in the 1 to 345 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

查看别名

TRBP, RISC-loading complex subunit TARBP2, TAR RNA-binding protein 2, Trans-activation-responsive RNA-binding protein

1 Images
SDS-PAGE - Recombinant Human TRBP protein (denatured) (Tag Free) (AB181920)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human TRBP protein (denatured) (Tag Free) (AB181920)

15% SDS PAGE analysis of ab181920 (3μg).

关键信息

纯度

>85% SDS-PAGE

表达系统

Escherichia coli

标签

Tag free

应用

SDS-PAGE

applications

生物活性

No

访问

Q15633

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

序列信息

[{"linker":null,"sequence":"MLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPVFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEVEPDDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCRVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCHGSATTREAARGEAARRALQYLKIMAGSK","proteinLength":"Full Length","predictedMolecularWeight":"36.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":345,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q15633","tags":[]}]

性能和储存信息

形式
Liquid
运输条件
Blue Ice
推荐的短期储存时间
1-2 weeks
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

Transactivation response RNA-binding protein (TRBP) also known as TARBP2 is a protein with a molecular weight of approximately 39 kDa. It is widely expressed in various tissues and plays a role in the RNA interference (RNAi) pathway. TRBP binds to double-stranded RNA and aids in the processing of microRNA (miRNA) by interacting with proteins such as Dicer and Argonaute. This protein participates significantly in the regulation of gene expression by influencing the stability and translation of target mRNAs.
Biological function summary

TRBP acts as a section of the RNA-induced silencing complex (RISC) where it directly interacts with Dicer and facilitates the maturation of miRNA precursors into their active forms. Through these interactions TRBP helps control diverse biological processes including cell growth differentiation and apoptosis. Its role in miRNA processing highlights its importance in maintaining cellular homeostasis. TRBP’s interactions extend beyond Dicer as it also stabilizes protein structures through its ability to homodimerize.

Pathways

TRBP contributes to the miRNA-mediated gene silencing pathway and the RNAi pathway. It works closely with proteins such as Dicer and Argonaute to ensure the effective formation of miRNA mature strands. TRBP's participation in these pathways links it with key cellular processes and suggests its implication in gene regulatory networks. This functional involvement with miRNA highlights TRBP's role in regulating post-transcriptional gene silencing adding layers of control over gene expression that are critical to normal cellular function.

TRBP has associations with cancer and neurological disorders. In cancer TRBP can regulate tumor suppressor miRNAs and oncogenic miRNAs influencing tumor progression and metastasis. TRBP is also connected to Neurological disorders where its dysregulation may affect neuronal gene expression. These connections position TRBP as a significant player in pathological conditions and stress the importance of understanding its role for potential therapeutic strategies.

常规信息

功能

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 (By similarity) (PubMed : 15973356, PubMed : 16142218, PubMed : 16271387, PubMed : 16357216, PubMed : 16424907, PubMed : 17452327, PubMed : 18178619). Binds in vitro to the PRM1 3'-UTR (By similarity). Seems to act as a repressor of translation (By similarity). For some pre-miRNA substrates, may also alter the choice of cleavage site by DICER1 (PubMed : 23063653). Negatively regulates IRF7-mediated IFN-beta signaling triggered by viral infection by inhibiting the phosphorylation of IRF7 and promoting its 'Lys'-48-linked ubiquitination and degradation (PubMed : 30927622).. (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 (PubMed : 11438532, PubMed : 12475984, PubMed : 2011739). This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha (PubMed : 11438532). May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR (PubMed : 12475984). 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 (PubMed : 30626973).

序列相似性

Belongs to the TARBP2 family.

亚细胞定位

Nucleus

产品实验方案

靶点信息

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 (By similarity) (PubMed : 15973356, PubMed : 16142218, PubMed : 16271387, PubMed : 16357216, PubMed : 16424907, PubMed : 17452327, PubMed : 18178619). Binds in vitro to the PRM1 3'-UTR (By similarity). Seems to act as a repressor of translation (By similarity). For some pre-miRNA substrates, may also alter the choice of cleavage site by DICER1 (PubMed : 23063653). Negatively regulates IRF7-mediated IFN-beta signaling triggered by viral infection by inhibiting the phosphorylation of IRF7 and promoting its 'Lys'-48-linked ubiquitination and degradation (PubMed : 30927622).. (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 (PubMed : 11438532, PubMed : 12475984, PubMed : 2011739). This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha (PubMed : 11438532). May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR (PubMed : 12475984). 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 (PubMed : 30626973).
See full target information TARBP2

文献 (1)

Recent publications for all applications. Explore the full list and refine your search

PloS one 10:e0120614 PubMed25793518

2015

DICER-ARGONAUTE2 complex in continuous fluorogenic assays of RNA interference enzymes.

Applications

Unspecified application

Species

Unspecified reactive species

Mark A Bernard,Leyu Wang,Souvenir D Tachado
View all publications

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