Description:

    Size: 100ul

    Catalog no.: bs-3896R-A594

    Price: 380 EUR

    Product details

    Gene ID Number

    9973

    Modification Site

    None

    Target Antigen

    SOD4/CCS

    Tested applications

    IF(IHC-P)

    French translation

    anticorps

    Modification

    Unmodified

    Clonality

    Polyclonal

    Excitation emission

    590nm/617nm

    Concentration

    1ug per 1ul

    Crossreactivity

    Human, Mouse, Rat

    Conjugated with

    ALEXA FLUOR® 594

    Conjugated

    Alexa conjugate 1

    Recommended dilutions

    IF(IHC-P)(1:50-200)

    Clone

    Polyclonal antibody

    Purification

    Purified by Protein A.

    Category

    Conjugated Primary Antibodies

    Conjugation

    Alexa Fluor,ALEXA FLUOR® 594

    Host Organism

    Rabbit (Oryctolagus cuniculus)

    Also known as

    Anti-SOD4/CCS PAb ALEXA FLUOR 594

    Specificity

    This is a highly specific antibody against SOD4/CCS.

    Long name

    SOD4/CCS Polyclonal Antibody, ALEXA FLUOR 594 Conjugated

    Cross-reactive species details

    Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.

    Source

    This antibody was obtained by immunization of the host with KLH conjugated synthetic peptide derived from human SOD4

    Synonyms

    CCS; CCS_HUMAN; Copper chaperone for superoxide dismutase; MGC138260; SOD 4; SOD4; Superoxide dismutase copper chaperone.

    Storage conditions

    Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.

    Properties

    For facs or microscopy Alexa 1 conjugate.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.

    Background of the antigen

    Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.