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MBOAT2 Protein (AA 1-519) (Strep Tag)

This Recombinant MBOAT2 protein is expressed in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3136657

Quick Overview for MBOAT2 Protein (AA 1-519) (Strep Tag) (ABIN3136657)

Target

See all MBOAT2 Proteins
MBOAT2 (Membrane Bound O-Acyltransferase Domain Containing 2 (MBOAT2))

Protein Type

Recombinant

Origin

  • 3
  • 1
Mouse

Source

  • 2
  • 1
  • 1
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
  • Protein Characteristics

    AA 1-519

    Purification tag / Conjugate

    This MBOAT2 protein is labelled with Strep Tag.

    Sequence

    MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQQ CCFVFALGYL SVCQITRVYI FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY TCNFMGILAG PLCSYKDYIA FIEGRASHVA QPSENGKDEQ HGKADPSPNA AVTEKLLVCG LSLLFHLTIS NMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP TIQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFLEPPQLK LFYDLITWVA TQITISYTVV PFVLLSIKPS FTFYSSWYYC LHVCSILVLL LLPVKKSQRR TSTQENVHLS QAKKFDERDN PLGQNSFSTM NNVCNQNRDT GSRHSSLTQ
    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®).
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  • 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
  • Target

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

    Alternative Name

    Mboat2

    Background

    Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (mLPCAT4) (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:18287005, PubMed:29196633). Catalyzes the acylation of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) (PubMed:18287005, PubMed:29196633). Does not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine (PubMed:18287005). Prefers oleoyl-CoA as the acyl donor (PubMed:18287005, PubMed:29196633). May be involved in chondrocyte differentiation (PubMed:29196633). {ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:29196633}.

    Molecular Weight

    59.0 kDa

    UniProt

    Q8R3I2
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