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Liver Arginase Protein (AA 1-323) (Strep Tag)

Crystallography grade ARG1 Origin: Mouse Host: Tobacco (Nicotiana tabacum) Recombinant ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. SDS, ELISA, WB
Catalog No. ABIN3122891
  • Target See all Liver Arginase (ARG1) Proteins
    Liver Arginase (ARG1) (Arginase, Liver (ARG1))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-323
    Origin
    • 11
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    Mouse
    Source
    • 6
    • 5
    • 5
    • 1
    • 1
    Tobacco (Nicotiana tabacum)
    Purification tag / Conjugate
    This Liver Arginase protein is labelled with Strep Tag.
    Application
    SDS-PAGE (SDS), ELISA, Western Blotting (WB)
    Sequence
    MSSKPKSLEI IGAPFSKGQP RGGVEKGPAA LRKAGLLEKL KETEYDVRDH GDLAFVDVPN DSSFQIVKNP RSVGKANEEL AGVVAEVQKN GRVSVVLGGD HSLAVGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVSFLLK ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPAF TPATGTPVLG GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTAEEVK STVNTAVALT LACFGTQREG NHKPGTDYLK PPK
    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
    Top Product
    Discover our top product ARG1 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. 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
    Liver Arginase (ARG1) (Arginase, Liver (ARG1))
    Alternative Name
    Arg1 (ARG1 Products)
    Synonyms
    SI:zC146F4.4 (novel protein with NUDIX domain) Protein, si:ch211-146f4.3 Protein, argi1 Protein, AI Protein, AI256583 Protein, Arg-1 Protein, PGIF Protein, arginase 1 Protein, arginase Protein, Arginase-1 Protein, arginase, liver Protein, L-arginase Protein, arg1 Protein, PGTG_16455 Protein, argi1 Protein, ARG1 Protein, Arg1 Protein
    Background
    Arginase-1 (EC 3.5.3.1) (Liver-type arginase) (Type I arginase),FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively, the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. {ECO:0000305}., FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (By similarity). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (PubMed:27043409). Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation, the regulatory outcome seems to be organ specific (PubMed:7537672, PubMed:19360123, PubMed:20483789, PubMed:23552798, PubMed:23637937). In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity (PubMed:19414774, PubMed:23248265). {ECO:0000250|UniProtKB:P05089, ECO:0000269|PubMed:15313928, ECO:0000269|PubMed:19360123, ECO:0000269|PubMed:19414774, ECO:0000269|PubMed:20483789, ECO:0000269|PubMed:23248265, ECO:0000269|PubMed:23552798, ECO:0000269|PubMed:23637937, ECO:0000269|PubMed:27043409, ECO:0000269|PubMed:7537672}.
    Molecular Weight
    34.8 kDa
    UniProt
    Q61176
    Pathways
    Cellular Response to Molecule of Bacterial Origin
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