EEFSEC Protein (AA 1-583) (Strep Tag)

Catalog No. ABIN3130014

Product Details

Target: EEFSEC (Eukaryotic Elongation Factor, Selenocysteine-tRNA-Specific (EEFSEC))

Protein Type: Recombinant

Protein Characteristics: AA 1-583

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

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

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

Sequence: MAGRRVNVNV GVLGHIDSGK TALARALSTT ASTAAFDKQP QSRERGITLD LGFSCFVVPL PGAEPGSSDT LLQVTLVDCP GHASLIRTII GGAQIIDLMM LVIDVTKGMQ TQSAECLVIG QIACQKLVVV LNKIDLLAEG KRQAAIDKMT KKMQKTLENT KFRGAPIIPV AAKPGGPEAP ETEAPQGISE LIELLKSQIS IPTRDPSGPF LMSVDHCFSI KGQGTVMTGT ILSGTISLGD SVEIPALKVV KKVKSMQMFH TPVTSAMQGD RLGICVTQFD PKLLERGLVC APESLHTVHA ALISVEKIPY FRGPLQTKAK FHITVGHETV MGRTLFFSPA PDSFDLEPVL DSFDLSREYL FQEQYLCKDS MPTATEGDDE ADPKAGHAPG GHCPRQQWAL VEFEKPVTCP RLCLVIGSRL DADIHTNTCR LAFHGVLLQG LEDKNYIESF LPALRVYKLK HKHGLVERVM DDYSVIGRSL FKKETNIQLF VGLKVQLSTG EQGIIDSAFG QSGKFKIHIP GGLSPESKKI LTPTLKKRSR AGRGETTKPE EGTERPEPIQ PVTLNLSFKR YVFDTQKRMV QTP
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: EEFSEC (Eukaryotic Elongation Factor, Selenocysteine-tRNA-Specific (EEFSEC))

Alternative Name: Eefsec (EEFSEC Products)

Synonyms: RGD1560552 Protein, EFSEC Protein, SELB Protein, Selb Protein, sec Protein, eukaryotic elongation factor, selenocysteine-tRNA-specific Protein, eukaryotic elongation factor, selenocysteine-tRNA specific Protein, Eefsec Protein, EEFSEC Protein

Background: Selenocysteine-specific elongation factor (EC 3.6.5.-) (Elongation factor sec) (Eukaryotic elongation factor, selenocysteine-tRNA-specific) (mSelB),FUNCTION: Translation factor required for the incorporation of the rare amino acid selenocysteine encoded by UGA codons (PubMed:11265756, PubMed:10970870, PubMed:22992746). Replaces the eRF1-eRF3-GTP ternary complex for the insertion of selenocysteine directed by the UGA codon (PubMed:11265756, PubMed:10970870, PubMed:22992746). Insertion of selenocysteine at UGA codons is mediated by SECISBP2 and EEFSEC: SECISBP2 (1) specifically binds the SECIS sequence once the 80S ribosome encounters an in-frame UGA codon and (2) contacts the RPS27A/eS31 of the 40S ribosome before ribosome stalling (By similarity). (3) GTP-bound EEFSEC then delivers selenocysteinyl-tRNA(Sec) to the 80S ribosome and adopts a preaccommodated state conformation (By similarity). (4) After GTP hydrolysis, EEFSEC dissociates from the assembly, selenocysteinyl-tRNA(Sec) accommodates, and peptide bond synthesis and selenoprotein elongation occur (By similarity). {ECO:0000250|UniProtKB:P57772, ECO:0000269|PubMed:10970870, ECO:0000269|PubMed:11265756, ECO:0000269|PubMed:22992746}.

Molecular Weight: 63.5 kDa

UniProt: Q9JHW4