TRIM39 Protein (AA 1-518) (Strep Tag)

Catalog No. ABIN3074890

This Recombinant TRIM39 protein is expressed in Cell-free protein synthesis (CFPS).

Quick Overview for TRIM39 Protein (AA 1-518) (Strep Tag) (ABIN3074890)

Target: TRIM39 (Tripartite Motif Containing 39 (TRIM39))

Protein Type: Recombinant

Origin: Human

Source: Cell-free protein synthesis (CFPS)

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

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

Grade: custom-made

Product Details

Protein Characteristics: AA 1-518

Purification tag / Conjugate: This TRIM39 protein is labelled with Strep Tag.

Sequence: MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK IRDESLCPQH HEALSLFCYE DQEAVCLICA ISHTHRAHTV VPLDDATQEY KEKLQKCLEP LEQKLQEITR CKSSEEKKPG ELKRLVESRR QQILREFEEL HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL AHLAAEVEGK CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL VLSEDRKSVK FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE
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: TRIM39 (Tripartite Motif Containing 39 (TRIM39))

Alternative Name: TRIM39

Background: E3 ubiquitin-protein ligase TRIM39 (EC 2.3.2.27) (RING finger protein 23) (RING-type E3 ubiquitin transferase TRIM39) (Testis-abundant finger protein) (Tripartite motif-containing protein 39),FUNCTION: [Isoform 1]: E3 ubiquitin-protein ligase (PubMed:22529100). May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1 (PubMed:19100260, PubMed:22529100). Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251). {ECO:0000269|PubMed:19100260, ECO:0000269|PubMed:22529100, ECO:0000269|PubMed:23213251}., FUNCTION: [Isoform 2]: Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251). Negatively regulates the canonical NF-kappa-B signaling pathway via stabilization of CACTIN in an ubiquitination-independent manner (PubMed:26363554). {ECO:0000269|PubMed:23213251, ECO:0000269|PubMed:26363554}.

Molecular Weight: 59.7 kDa

UniProt: Q9HCM9