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: Cell-free protein synthesis (CFPS)

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

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

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 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®).

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

Grade: custom-made

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

Alternative Name: Bard1 (BARD1 Products)

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