TARBP2 Protein (AA 1-345)
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- Target See all TARBP2 Proteins
- TARBP2 (TAR (HIV-1) RNA Binding Protein 2 (TARBP2))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-345
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Application
- SDS-PAGE (SDS)
- Sequence
- MLAANPGKTP ISLLQEYGTR IGKTPVYDLL KAEGQAHQPN FTFRVTVGDT SCTGQGPSKK AAKHKAAEVA LKHLKGGSML EPALEDSSSF SPLDSSLPED IPVFTAAAAA TPVPSVVLTR SPPMELQPPV SPQQSECNPV GALQELVVQK GWRLPEYTVT QESGPAHRKE FTMTCRVERF IEIGSGTSKK LAKRNAAAKM LLRVHTVPLD ARDGNEVEPD DDHFSIGVGS RLDGLRNRGP GCTWDSLRNS VGEKILSLRS CSLGSLGALG PACCRVLSEL SEEQAFHVSY LDIEELSLSG LCQCLVELST QPATVCHGSA TTREAARGEA ARRALQYLKI MAGSK
- Purity
- > 85 % by SDS - PAGE
- Top Product
- Discover our top product TARBP2 Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Comment
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Denatured
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- Liquid. In 20 mM Tris-HCl buffer ( pH 8.0) containing 10 % glycerol 0.4M urea
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.
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- Target
- TARBP2 (TAR (HIV-1) RNA Binding Protein 2 (TARBP2))
- Alternative Name
- TARBP2 (TARBP2 Products)
- Background
- TARBP2 is a component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, EIF2C2/AGO2 and TARBP2. This protein contains 3 DRBM (double-stranded RNA-binding) domains. It may also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. TARBP2 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. Recombinant human TARBP2 protein was expressed in E.coli.
- Molecular Weight
- 36.9 kDa (345aa)
- NCBI Accession
- NP_004169
- UniProt
- Q15633
- Pathways
- Regulatory RNA Pathways, Ribonucleoprotein Complex Subunit Organization
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