BARD1 Protein (AA 1-765) (Strep Tag)

Catalog No. ABIN3132003

Product Details

Target: BARD1 (BRCA1 Associated RING Domain 1 (BARD1))

Protein Type: Recombinant

Protein Characteristics: AA 1-765

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This BARD1 protein is labelled with Strep Tag.

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

Sequence: MPRRPPRVCS GNQPAPVPAM EPATDGLWAH SRAALARLEK LLRCSRCANI LKEPVCLGGC EHIFCSGCIS DCVGSGCPVC YTPAWILDLK INRQLDSMIQ LSSKLQNLLH DNKDSKDNTS RASLFGDAER KKNSIKMWFS PRSKKVRYVV TKVSVQTQPQ KAKDDKAQEA SMYEFVSATP PVAVPKSAKT ASRTSAKKHP KKSVAKINRE ENLRPETKDS RFDSKEELKE EKVVSCSQIP VMERPRVNGE IDLLASGSVV EPECSGSLTE VSLPLAEHIV SPDTVSKNEE TPEKKVCVKD LRSGGSNGNR KGCHRPTTST SDSCGSNIPS TSRGIGEPAL LAENVVLVDC SSLPSGQLQV DVTLRRKSNA SDDPLSLSPG TPPPLLNNST HRQMMSSPST VKLSSGMPAR KRNHRGETLL HIASIKGDIP SVEYLLQNGN DPNVKDHAGW TPLHEACSHG HLKVVELLLQ HNALVNTPGY QNDSPLHDAV KSGHIDIVKV LLSHGASRNA VNIFGVRPVD YTDNENIRSL LLLPEENESF STSQCSIVNT GQRKNGPLVF IGSGLSSQQQ KMLSKLETVL KAKKCMEFDS TVTHVIVPDE EAQSTLKCML GILSGCWILK FDWVKACLDS KVREQEEKYE VPGGPQRSRL NREQLLPKLF DGCYFFLGGN FKHHPRDDLL KLIAAAGGKV LSRKPKPDSD VTQTINTVAY HAKPESDQRF CTQYIVYEDL FNCHPERVRQ GKVWMAPSTW LISCIMAFEL LPLDS
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: BARD1 (BRCA1 Associated RING Domain 1 (BARD1))

Alternative Name: Bard1 (BARD1 Products)

Synonyms: BARD1 Protein, LOC100147913 Protein, ENSMUSG00000060893 Protein, ENSMUSG00000073653 Protein, BRCA1 associated RING domain 1 Protein, BARD1 Protein, bard1 Protein, Bard1 Protein

Background: BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1),FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. {ECO:0000250|UniProtKB:Q99728}.

Molecular Weight: 84.3 kDa

UniProt: O70445

Pathways: DNA Damage Repair