FEN1 Protein (AA 1-380) (Strep Tag)
Quick Overview for FEN1 Protein (AA 1-380) (Strep Tag) (ABIN3092557)
Target
See all FEN1 ProteinsProtein Type
Origin
Source
Application
Purity
Grade
-
-
Protein Characteristics
- AA 1-380
-
Purification tag / Conjugate
- This FEN1 protein is labelled with Strep Tag.
-
Sequence
-
MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK
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®).
-
-
Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System Wheat germConjugate GST tagOrigin HumanPrice $481.06Expression System Escherichia coli (E. coli)ConjugateOrigin HumanPrice $457.60Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $663.94Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $561.51Expression System HEK-293 CellsConjugate Myc-DYKDDDDK TagOrigin HumanPrice $748.80Your project requires further customization? Contact us and discover our custom protein solutions
-
-
-
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
-
-
-
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
-
-
- FEN1 (Flap Structure-Specific Endonuclease 1 (FEN1))
-
Alternative Name
- FEN1
-
Background
- Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNase IV) (Flap structure-specific endonuclease 1) (Maturation factor 1) (MF1) (hFEN-1),FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741, ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037, ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:26751069, ECO:0000269|PubMed:7961795, ECO:0000269|PubMed:8621570}.
-
Molecular Weight
- 42.6 kDa
-
UniProt
- P39748
-
Pathways
- Telomere Maintenance, DNA Damage Repair, DNA Replication, Synthesis of DNA
Target
-