MBOAT2 Protein (AA 1-520) (Strep Tag)

Catalog No. ABIN3115919

Recombinant MBOAT2 protein expressed in Cell-free protein synthesis (CFPS).

Quick Overview for MBOAT2 Protein (AA 1-520) (Strep Tag) (ABIN3115919)

Target: MBOAT2 (Membrane Bound O-Acyltransferase Domain Containing 2 (MBOAT2))

Protein Type: Recombinant

Origin: Human

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 1-520

Purification tag / Conjugate: This MBOAT2 protein is labelled with Strep Tag.

Sequence: MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK TSSFIRHVVA TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN YCFVFALGYL TVCQVTRVYI FDYGQYSADF SGPMMIITQK ITSLACEIHD GMFRKDEELT SSQRDLAVRR MPSLLEYLSY NCNFMGILAG PLCSYKDYIT FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC GLSLLFHLTI CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK RVCYERTSFS PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF RHYFIEPSQL KLFYDVITWI VTQVAISYTV VPFVLLSIKP SLTFYSSWYY CLHILGILVL LLLPVKKTQR RKNTHENIQL SQSKKFDEGE NSLGQNSFST TNNVCNQNQE IASRHSSLKQ
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: MBOAT2 (Membrane Bound O-Acyltransferase Domain Containing 2 (MBOAT2))

Alternative Name: MBOAT2

Background: Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphate O-acyltransferase MBOAT2) (EC 2.3.1.51) (1-acylglycerophosphocholine O-acyltransferase MBOAT2) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine MBOAT2 O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidic acid acyltransferase) (LPAAT) (Lyso-PA acyltransferase) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2),FUNCTION: Acyltransferase which catalyzes the transfer of an acyl group from an acyl-CoA to a lysophospholipid leading to the production of a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (PubMed:18772128). Catalyzes preferentially the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) and lysophosphatidic acid (LPA) and to a lesser extend lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS) (PubMed:18772128). Prefers oleoyl-CoA as the acyl donor (PubMed:18772128). May be involved in chondrocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q8R3I2, ECO:0000269|PubMed:18772128}.

Molecular Weight: 59.5 kDa

UniProt: Q6ZWT7