EPHX2 Protein (AA 1-554) (Strep Tag)
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- Antigène Voir toutes EPHX2 Protéines
- EPHX2 (Epoxide Hydrolase 2, Cytoplasmic (EPHX2))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-554
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Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette EPHX2 protéine est marqué à la Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Séquence
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MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT EQLMKGKITF SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS INRPMLQAAI ALKKKGFTTC IVTNNWLDDG DKRDSLAQMM CELSQHFDFL IESCQVGMIK PEPQIYNFLL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV TVKPGIRLHF VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV RAVASLNTPF MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS RTFKSFFRAS DETGFIAVHK ATEIGGILVN TPEDPNLSKI TTEEEIEFYI QQFKKTGFRG PLNWYRNTER NWKWSCKGLG RKILVPALMV TAEKDIVLRP EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW LQTEVQNPSV TSKI
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. - Attributs du produit
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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
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Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
- 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.
- 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.
- Pureté
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- niveau d'endotoxine
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Top Product
- Discover our top product EPHX2 Protéine
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- Indications d'application
- 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.
- Commentaires
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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
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
- Conseil sur la manipulation
- Avoid repeated freeze-thaw cycles.
- Stock
- -80 °C
- Stockage commentaire
- Store at -80°C.
- Date de péremption
- Unlimited (if stored properly)
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- Antigène
- EPHX2 (Epoxide Hydrolase 2, Cytoplasmic (EPHX2))
- Autre désignation
- Ephx2 (EPHX2 Produits)
- Synonymes
- CEH Protein, SEH Protein, Eph2 Protein, sEP Protein, epoxide hydrolase 2 Protein, soluble epoxide hydrolase Protein, Soluble epoxide hydrolase Protein, alpha/beta hydrolase Protein, epoxide hydrolase 2, cytoplasmic Protein, EPHX2 Protein, SEH2 Protein, PTRG_01276 Protein, Deima_0402 Protein, Deipr_0144 Protein, Psed_0418 Protein, Fluta_3767 Protein, HALXA_RS12710 Protein, Ephx2 Protein
- Sujet
- Bifunctional epoxide hydrolase 2 [Includes: Cytosolic epoxide hydrolase 2 (CEH) (EC 3.3.2.10) (Epoxide hydratase) (Soluble epoxide hydrolase) (SEH), Lipid-phosphate phosphatase (EC 3.1.3.76)],FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:7840649, PubMed:21217101). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (By similarity). {ECO:0000250|UniProtKB:P34913, ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:7840649}., FUNCTION: Bifunctional enzyme. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid (By similarity). Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (By similarity). {ECO:0000250|UniProtKB:P34913}.
- Poids moléculaire
- 62.5 kDa
- UniProt
- P34914
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