Spartan Protein (AA 1-497) (Strep Tag)

Catalog No. ABIN3131201

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

Quick Overview for Spartan Protein (AA 1-497) (Strep Tag) (ABIN3131201)

Target: Spartan (C1orf124) (Chromosome 1 Open Reading Frame 124 (C1orf124))

Protein Type: Recombinant

Origin: Mouse

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 1-497

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

Sequence: MDEDLVVALR LQEEWDVQMA RRAAAAREPV SLVDASWELV DPTPDLQALF LQFNDRFFWG QLEAVEVKWS VRMTLCAGIC TYEGRGGMCS IRLSEPLLKL RPRKDLVETL LHEMIHAYLF VTNNDKDREG HGPEFCKHMH RINQLTGANI TVYHTFHDEV DEYRRHWWRC NGPCQHRQPY YGYVKRATNR APSVHDYWWA DHQKTCGGTY IKIKEPENYS KKGRGKTKAD KQPASAVENK DKLCRGEAQL LIPFSGKGYV LGDASTCPSA GKLNTSYMVN EAKGLSSQDH SVSGLRLNSN AEVKCEQNCL PKKPHLVSPL PTASHQSVLS SYFPRVSVAN QKAFRNVNGS PVKNGTTGDG TKRPASGGSQ RKVPPSRASL RNTSKVTAPA SATVTSAAGT SATISREESG SEDQFLNKRP RLEDRTALDT IKEQTQSGGD LRSSSQPTAA SAPQSLSSQR RLVNCPVCQG VVVESQINEH LDRCLEGNKT NLRPRRV
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: Spartan (C1orf124) (Chromosome 1 Open Reading Frame 124 (C1orf124))

Alternative Name: Sprtn

Background: DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan),FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:28199696, PubMed:27871365). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed:28199696, PubMed:27871365). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (By similarity). Catalyzes proteolytic cleavage of the HMCES DNA-protein cross-link following unfolding by the BRIP1/FANCJ helicase (By similarity). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity). {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040, ECO:0000269|PubMed:27871365, ECO:0000269|PubMed:28199696}.

Molecular Weight: 55.3 kDa

UniProt: G3X912