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RAD23B antibody (N-Term)

RAD23B Reactivity: Human, Mouse, Rat WB Host: Mouse Monoclonal 1228CT409-120-123-135 unconjugated
Catalog No. ABIN1944896
  • Target See all RAD23B Antibodies
    RAD23B (RAD23 Homolog B (RAD23B))
    Binding Specificity
    • 15
    • 11
    • 7
    • 6
    • 5
    • 5
    • 4
    • 4
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 1-409, N-Term
    Reactivity
    • 73
    • 30
    • 30
    • 6
    • 6
    • 4
    • 4
    • 4
    • 4
    • 3
    • 3
    • 2
    • 2
    • 1
    Human, Mouse, Rat
    Host
    • 56
    • 16
    • 1
    Mouse
    Clonality
    • 58
    • 15
    Monoclonal
    Conjugate
    • 45
    • 5
    • 4
    • 4
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    This RAD23B antibody is un-conjugated
    Application
    • 65
    • 30
    • 24
    • 15
    • 14
    • 13
    • 13
    • 9
    • 7
    • 3
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    Western Blotting (WB)
    Purification
    This antibody is purified through a protein G column, followed by dialysis against PBS.
    Immunogen
    This RAD23B antibody is generated from a mouse immunized with a KLH conjugated synthetic peptide between 1-409 amino acids from the N-terminal region of human RAD23B.
    Clone
    1228CT409-120-123-135
    Isotype
    IgG1 kappa
    Top Product
    Discover our top product RAD23B Primary Antibody
  • Application Notes
    WB: 1:1000
    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    Purified monoclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
    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
    4 °C,-20 °C
    Expiry Date
    6 months
  • Huang, Wang, Xu, Lu, Xu, Li, Zhou, Sha: "Expression of a novel RAD23B mRNA splice variant in the human testis." in: Journal of andrology, Vol. 25, Issue 3, pp. 363-8, (2004) (PubMed).

    Humphray, Oliver, Hunt, Plumb, Loveland, Howe, Andrews, Searle, Hunt, Scott, Jones, Ainscough, Almeida, Ambrose, Ashwell, Babbage, Babbage, Bagguley, Bailey, Banerjee, Barker, Barlow, Bates, Beasley et al.: "DNA sequence and analysis of human chromosome 9. ..." in: Nature, Vol. 429, Issue 6990, pp. 369-74, (2004) (PubMed).

    Masutani, Sugasawa, Yanagisawa, Sonoyama, Ui, Enomoto, Takio, Tanaka, van der Spek, Bootsma: "Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23." in: The EMBO journal, Vol. 13, Issue 8, pp. 1831-43, (1994) (PubMed).

  • Target
    RAD23B (RAD23 Homolog B (RAD23B))
    Alternative Name
    RAD23B (RAD23B Products)
    Synonyms
    HHR23B antibody, HR23B antibody, P58 antibody, 0610007D13Rik antibody, AV001138 antibody, mHR23B antibody, p58 antibody, MGC107846 antibody, zgc:65951 antibody, RAD23 homolog B, nucleotide excision repair protein antibody, UV excision repair protein RAD23 homolog B antibody, RAD23 homolog B, nucleotide excision repair protein S homeolog antibody, RAD23B antibody, Rad23b antibody, rd23b antibody, rad23b antibody, rad23b.S antibody
    Background
    Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER, it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
    Molecular Weight
    43171
    Gene ID
    5887
    UniProt
    P54727
    Pathways
    DNA Damage Repair
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