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APEH Protein (AA 1-732) (Strep Tag)

custom-made APEH Origin: Mouse Host: Cell-free protein synthesis (CFPS) Recombinant > 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC). ELISA, WB, SDS
Catalog No. ABIN3126598
  • Target See all APEH Proteins
    APEH (N-Acylaminoacyl-Peptide Hydrolase (APEH))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-732
    Origin
    • 3
    • 1
    • 1
    Mouse
    Source
    • 2
    • 1
    • 1
    • 1
    Cell-free protein synthesis (CFPS)
    Purification tag / Conjugate
    This APEH protein is labelled with Strep Tag.
    Application
    ELISA, Western Blotting (WB), SDS-PAGE (SDS)
    Brand
    AliCE®
    Sequence
    MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLDRMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GAVSGEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK ALDVSASDEE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDIE SGNISVLEGV PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDESL AVCSPRLSPD QCRVVYLQYP SLAPHHQCSQ LFLYDWYTKV TSLVVDIVPR QLGESFSGIY CSLLPLGCWS ADSQRVVFDS VQRSRQDLFA VDTQTGSVTS LTAGGSAGSW KLLTIDRDLM VAQFSTPNLP PSLKVGFLPP AGKEQSVSWV SLEEAEPIPD IHWGIRVLHP PPDQENVQYA DLDFEAILLQ PSNSPDKSQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS LPGNVGHQDV KDVQFAVQQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY PETYSACIAR NPVINIVSMM GTTDIPDWCM VETGFPYSND YLPDLNVLEE MLDKSPIKYI PQVKTPVLLM LGQEDRRVPF KQGLEYYHAL KARNVPVRLL LYPKSTHALS EVEVESDSFM NTVLWLHTHL GS
    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 in one-step affinity chromatography
    • 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 try to ensure that you receive soluble 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 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®).
    Purity
    > 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
    Grade
    custom-made
    Top Product
    Discover our top product APEH Protein
  • 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
    APEH (N-Acylaminoacyl-Peptide Hydrolase (APEH))
    Alternative Name
    Apeh (APEH Products)
    Background
    Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Acyl-peptide hydrolase) (APH) (Acylaminoacyl-peptidase),FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus (By similarity). It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Also, involved in the degradation of oxidized and glycated proteins (By similarity). {ECO:0000250|UniProtKB:P13676, ECO:0000250|UniProtKB:P13798}.
    Molecular Weight
    81.6 kDa
    UniProt
    Q8R146
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