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RAD23B antibody (N-Term)

The Mouse Monoclonal anti-RAD23B antibody has been validated for WB. It is suitable to detect RAD23B in samples from Human, Mouse and Rat. There are 3+ publications available.
Catalog No. ABIN1944896

Quick Overview for RAD23B antibody (N-Term) (ABIN1944896)

Target

See all RAD23B Antibodies
RAD23B (RAD23 Homolog B (RAD23B))

Reactivity

  • 87
  • 37
  • 35
  • 6
  • 6
  • 4
  • 4
  • 4
  • 4
  • 3
  • 3
  • 2
  • 2
  • 1
Human, Mouse, Rat

Host

  • 67
  • 19
  • 1
Mouse

Clonality

  • 68
  • 19
Monoclonal

Conjugate

  • 52
  • 4
  • 3
  • 3
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
This RAD23B antibody is un-conjugated

Application

  • 67
  • 30
  • 26
  • 16
  • 15
  • 14
  • 13
  • 13
  • 10
  • 3
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
Western Blotting (WB)

Clone

1228CT409-120-123-135
  • Binding Specificity

    • 15
    • 7
    • 7
    • 6
    • 5
    • 4
    • 4
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 1-409, N-Term

    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.

    Isotype

    IgG1 kappa
  • 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

    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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