TARBP2 Protein (AA 1-366) (Strep Tag)
Quick Overview for TARBP2 Protein (AA 1-366) (Strep Tag) (ABIN3095987)
Target
See all TARBP2 ProteinsProtein Type
Origin
Source
Application
Purity
Grade
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Protein Characteristics
- AA 1-366
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Purification tag / Conjugate
- This TARBP2 protein is labelled with Strep Tag.
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Sequence
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MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE DIPVFTAAAA ATPVPSVVLT RSPPMELQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV TQESGPAHRK EFTMTCRVER FIEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEVEP DDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCRVLSE LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS ATTREAARGE AARRALQYLK IMAGSK
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us.. -
Characteristics
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Key Benefits:
- Made in Germany - from design to production - by highly experienced protein experts.
- Protein expressed with ALiCE® and purified in one-step affinity chromatography
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.
The big advantage of ordering our predefined custom proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
Expression System:- ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
- During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!
Concentration:- The concentration of our recombinant proteins is measured using the absorbance at 280nm.
- The protein's absorbance will be measured against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
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Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
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Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System Escherichia coli (E. coli)ConjugateOrigin HumanPrice $584.62Expression System Wheat germConjugate GST tagOrigin HumanPrice $823.16Expression System Escherichia coli (E. coli)Conjugate His-IF2DI TagOrigin HumanPrice $604.62Expression System Escherichia coli (E. coli)ConjugateOrigin HumanPrice $1,071.05Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $396.00Expression System BacteriaConjugate His tagOrigin HumanPrice $520.52Your project requires further customization? Contact us and discover our custom protein solutions
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Application Notes
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
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Comment
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ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein! -
Restrictions
- For Research Use only
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Format
- Liquid
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Buffer
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The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein. -
Handling Advice
- Avoid repeated freeze-thaw cycles.
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Storage
- -80 °C
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Storage Comment
- Store at -80°C.
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Expiry Date
- 12 months
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- TARBP2 (TAR (HIV-1) RNA Binding Protein 2 (TARBP2))
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Alternative Name
- TARBP2
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Background
- RISC-loading complex subunit TARBP2 (TAR RNA-binding protein 2) (Trans-activation-responsive RNA-binding protein),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 (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). {ECO:0000250|UniProtKB:P97473, ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:23063653, ECO:0000269|PubMed:30927622}., FUNCTION: (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:2011739, PubMed:11438532, PubMed:12475984). 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). {ECO:0000269|PubMed:11438532, ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:2011739, ECO:0000269|PubMed:30626973}.
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Molecular Weight
- 39.0 kDa
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UniProt
- Q15633
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Pathways
- Regulatory RNA Pathways, Ribonucleoprotein Complex Subunit Organization
Target
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