RAD23B Antibody (N-term) western blot analysis in A549 cell line lysates (35ug/lane).This demonstrates the RAD23B antibody detected the RAD23B protein (arrow).
RAD23B; UV excision repair protein RAD23 homolog B; XP-C repair-complementing complex 58 kDa protein
Key Feature
Clonality
Polyclonal
Isotype
Ig
Host Species
Rabbit
Tested Applications
WB
WB:1:100~500
Species Reactivity
Human
Concentration
1mg/ml
Target Information
Alternative Names
RAD23B UV excision repair protein RAD23 homolog B XP-C repair-complementing complex 58 kDa protein
Molecular Weight(MW)
43171 Da
Function
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
Tissue Specificity
This RAD23B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 10-40 amino acids from the N-terminal region of human RAD23B.
Cellular Localization
Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S- phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin
RAD23B Antibody (N-term) western blot analysis in A549 cell line lysates (35ug/lane).This demonstrates the RAD23B antibody detected the RAD23B protein (arrow).
Application Notes
WB:1:100~500
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Storage Buffer
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.