EPHX2 Protein (AA 1-555) (Strep Tag)

Catalog No. ABIN3093012

Product Details

Target: EPHX2 (Epoxide Hydrolase 2, Cytoplasmic (EPHX2))

Protein Type: Recombinant

Protein Characteristics: AA 1-555

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This EPHX2 protein is labelled with Strep Tag.

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

Sequence: MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP VVSKM
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: EPHX2 (Epoxide Hydrolase 2, Cytoplasmic (EPHX2))

Alternative Name: EPHX2 (EPHX2 Products)

Synonyms: 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

Background: 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 (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687, PubMed:21217101). {ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654, ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:22798687}., FUNCTION: Bifunctional enzyme (PubMed:12574510). 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 (PubMed:12574510). Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (PubMed:22217705, PubMed:22387545). {ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:22217705, ECO:0000269|PubMed:22387545}.

Molecular Weight: 62.6 kDa

UniProt: P34913