ADAR Protein (AA 1-1178) (Strep Tag)

Catalog No. ABIN3136977

This Recombinant ADAR protein is produced in Cell-free protein synthesis (CFPS).

Quick Overview for ADAR Protein (AA 1-1178) (Strep Tag) (ABIN3136977)

Target: ADAR (Adenosine Deaminase, RNA-Specific (ADAR))

Protein Type: Recombinant

Origin: Mouse

Source: Cell-free protein synthesis (CFPS)

Application: ELISA, SDS-PAGE (SDS), Western Blotting (WB)

Purity: approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Product Details

Protein Characteristics: AA 1-1178

Purification tag / Conjugate: This ADAR protein is labelled with Strep Tag.

Sequence: MSQGFRGPTG VFPHQTQSYL DPSHEHSKWR YPQPQGPESY PRSFQLQQIE FLKGRLPEAP LIGIQTQSLP PFLPGHWPRF PGPPAQDRQL EIWEFPRSVT LRNQGFHIGP PLPPPHSRGT PWRGADGLCS HFRELSISQS PEQKVLNRLE ELGEGKATTA HVLARELRIP KRDINRILYS LEKKGKLHRG RGKPPLWSLV PLSQAWTQPP GVVNPDSCIQ EFPRGEPGLD SEDGDPASDL EGPSEPLDMA EIKEKICDYL FNVSNSSALN LAKNIGLTKA RDVTSVLIDL ERQGDVYRQG ATPPIWYLTD KKRERLQMKR STHSAPAPTP TAVPEATRSP SFPACHPPPA GASSSVAASK RVENGQEPAI KHESRHEARP GPMRLRPHAY HNGPSRAGYV ASENGQWATD DIPDNLNSIH TAPGEFRAIM EMPSFYSPTL PRCSPYKKLT ECQLKNPVSG LLEYAQFTSQ TCDFNLIEQS GPSHEPRFKF QVVINGREFP PAEAGSKKVA KQDAAVKAMA ILLREAKAKD SGQPEDLSHC PMEEDSEKPA EAQAPSSSAT SLFSGKSPVT TLLECMHKLG NSCEFRLLSK EGPAHDPKFQ YCVAVGAQTF PPVSAPSKKV AKQMAAEEAM KALQEEAASS ADDQSGGANT DSLDESMAPN KIRRIGELVR YLNTNPVGGL LEYARSHGFA AEFKLIDQSG PPHEPKFVYQ AKVGGRWFPA VCAHSKKQGK QDAADAALRV LIGESEKAEQ LGFAEVTPVT GASLRRTMLL LSRSPDAHPK TLPLSGSTFH DQIAMLSHRC FNALTNSFQP SLLGRKILAA IIMKRDPEDM GVVVSLGTGN RCVKGDSLSL KGETVNDCHA EIISRRGFIR FLYSELMKYN HHTAKNSIFE LARGGEKLQI KKTVSFHLYI STAPCGDGAL FDKSCSDRAV ESTESRHYPV FENPKQGKLR TKVENGEGTI PVESSDIVPT WDGIRLGERL RTMSCSDKIL RWNVLGLQGA LLTHFLQPVY LKSVTLGYLF SQGHLTRAIC CRVTRDGKAF EDGLRYPFIV NHPKVGRVSV YDSKRQSGKT KETSVNWCMA DGYDLEILDG TRGTVDGPGK ELSRVSKKNI FLQFKKLCSF RARRDLLQLS YGEAKKAARD YDLAKNYFKK SLRDMGYGNW ISKPQEEKNF YLCPVPND
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: 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.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).

Application Details

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.

Comment:

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

Handling

Format: Liquid

Buffer: 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.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: ADAR (Adenosine Deaminase, RNA-Specific (ADAR))

Alternative Name: Adar

Background: Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (RNA adenosine deaminase 1),FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine, pre-mRNA splicing by altering splice site recognition sequences, RNA stability by changing sequences involved in nuclease recognition, genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication, and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Does not affect polyomavirus replication but provides protection against virus-induced cytopathic effects. Essential for embryonic development and cell survival and plays a critical role in the maintenance of hematopoietic stem cells. {ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:17369310}.

Molecular Weight: 130.4 kDa

UniProt: Q99MU3

Pathways: Protein targeting to Nucleus