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V5 Epitope Tag antibody Primary Antibody

Reactivity: Tag IP, ELISA, WB Host: Rabbit Polyclonal
Pubmed (5)
Catalog No. ABIN129577
$424.50
Plus shipping costs $45.00 and $22.00 dry ice
100 μg
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  • Target
    Reactivity
    Tag
    Host
    Rabbit
    Clonality
    Polyclonal
    Conjugate
    Un-conjugated
    Application
    Immunoprecipitation (IP), ELISA, Western Blotting (WB)
    Sequence
    GKPIPNPLLG LDST
    Characteristics
    Concentration Definition: by UV absorbance at 280 nm
    Immunogen
    This antibody was purified from whole rabbit serum prepared by repeated immunizations with V5 epitope tag peptide corresponding to aa 95-108 of the V protein conjugated to KLH using maleimide.
    Isotype
    IgG
  • Target
    Alternative Name
    V5-Tag
    Target Type
    Tag
    Background
    Epitope tags are short peptide sequences that are easily recognized by tag-specific antibodies.  Due to their small size, epitope tags do not affect the tagged protein’s biochemical properties.   Most often sequences encoding the epitope tag are included with target DNA at the time of cloning to produce fusion proteins containing the epitope tag sequence.  This allows anti-epitope tag antibodies to serve as universal detection reagents for any tag containing protein produced by recombinant means.  This means that anti-epitope tag antibodies are a useful alternative to generating specific antibodies to identify, immunoprecipitate or immunoaffinity purify a recombinant protein.  The anti-epitope tag antibody is usually functional in a variety of antibody-dependent experimental procedures.  Expression vectors producing epitope tag fusion proteins are available for a variety of host expression systems including bacteria, yeast, insect and mammalian cells.  Supplier produces anti-epitope tag antibodies against many common epitope tags including Myc, GST, GFP, 6X His, MBP, FLAG, HA and V5. Supplier also produces antibodies to other tags including FITC, Rhodamine (TRITC), DNP and biotin.
    Gene ID
    55775699
  • Application Notes
    Anti-V5 is optimally suited for monitoring expression of V5-tagged fusion proteins. The V5 epitope tag is derived from a small epitope (Pk) present on the P and V proteins of the paramyxovirus of simian virus 5 (SV5). The V5 tag is usually used with all 14 amino acids (GKPIPNPLLGLDST), although it has also been used with a shorter 9 amino acid sequence (IPNPLLGLD). This antibody has been tested by ELISA and western blotting against both the immunizing peptide and V5 containing recombinant proteins.  Although not tested, this antibody is likely functional for immunoprecipitation and immunocytochemistry.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    0.73 mg/mL
    Buffer
    0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
    Preservative
    Sodium azide
    Precaution of Use
    This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Storage
    -20 °C
  • Kotredes, Razmpour, Lutton, Alfonso-Prieto, Ramirez, Gamero: "Characterization of cancer-associated IDH2 mutations that differ in tumorigenicity, chemosensitivity and 2-hydroxyglutarate production." in: Oncotarget, Vol. 10, Issue 28, pp. 2675-2692, 2019 (PubMed).

    Schweiger, Clement, Page, Schepeler, Zou, Sirokmány, Watt, Jensen: "Lrig1 marks a population of gastric epithelial cells capable of long-term tissue maintenance and growth in vitro." in: Scientific reports, Vol. 8, Issue 1, pp. 15255, 2018 (PubMed).

    Glaeser, Urban, Fenech, Voloshanenko, Kranz, Lari, Christianson, Boutros: "ERAD-dependent control of the Wnt secretory factor Evi." in: The EMBO journal, Vol. 37, Issue 4, 2018 (PubMed).

    Watanabe, Simon, Durham, Kemp, Machihara, Kemal, Shi, Foley, Li, Chen, Weiser, Burger, Anastos, Chen, Carter: "The HIV-1 late domain-2 S40A polymorphism in antiretroviral (or ART)-exposed individuals influences protease inhibitor susceptibility." in: Retrovirology, Vol. 13, Issue 1, pp. 64, 2017 (PubMed).

    Huang, Li, Chen: "Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions." in: Retrovirology, Vol. 8, Issue 1, pp. 79, 2012 (PubMed).

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