RNF168 Protein (AA 1-565) (Strep Tag)

Catalog No. ABIN3136063

Product Details

Target: RNF168 (Ring Finger Protein 168 (RNF168))

Protein Type: Recombinant

Protein Characteristics: AA 1-565

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This RNF168 protein is labelled with Strep Tag.

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

Sequence: MAAPKTSIPS LAECQCGICM EILLEPVTLP CNHTLCNPCF QSTVEKANLC CPFCRRRVSS WTRYHTRRNS LVNTDLWEII QKHYAKECKL RISGQESKEI IDECQPVRRL SEPGELRREY EEEISRVEAE RQASKEEENK ASEEYIQRLL AEEEEEEKRQ REKRRSEMEE QLRGDEELAR SLSTSINSNY ERNTLASPLS SRKSDPVTNK SQKKNTSKQK TFGDIQKYLS PKLKPGTALA CKAELEEDIC KSKETDRSDT KSPVLQDTEI EKNIPTLSPQ TCLETQEQGS ESSAGIPGPQ LCVGDTKESL EGKVETVSTS PDDLCIVNDD GPRATVFYSN EAAVNSSSKI ENEEYSVTGV PQLTGGNRVP TESRVYHLLV EEEISDRENQ ESVFEEVMDP CFSAKRRKIF IESSSDQEET EVNFTQKLID LEHMLFERHK QEEQDRLLAL QLQKEVDKEQ MVPNRQKGSP DQYQLRTPSP PDRLLNRQRK NSKDRNSLQQ TNADHSKSPR NTKGDYWEPF KNTWKDSVNG TKMPTSTQDN CNVSKSAYTV QHRKSQRSIV QMFQR
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case 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 by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order 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 in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

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. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: RNF168 (Ring Finger Protein 168 (RNF168))

Alternative Name: Rnf168 (RNF168 Products)

Synonyms: 3110001H15Rik Protein, hRNF168 Protein, ring finger protein 168 Protein, ring finger protein 168, E3 ubiquitin protein ligase L homeolog Protein, Rnf168 Protein, rnf168.L Protein, RNF168 Protein

Background: E3 ubiquitin-protein ligase RNF168 (EC 2.3.2.27) (RING finger protein 168) (RING-type E3 ubiquitin transferase RNF168),FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro, possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066, ECO:0000269|PubMed:20080757}.

Molecular Weight: 64.8 kDa

UniProt: Q80XJ2

Pathways: Production of Molecular Mediator of Immune Response