Rad23b Polyclonal Antibody Catalog # AP72145

10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609

Rad23B Polyclonal Antibody Catalog # AP72145

Specification

Rad23B Polyclonal Antibody - Product Information

Application WB Primary Accession P54727 Reactivity Human, Mouse, Rat Host Rabbit Clonality Polyclonal

Rad23B Polyclonal Antibody - Additional Information

Gene ID 5887

Other Names RAD23B; UV excision repair protein RAD23 homolog B; HR23B; hHR23B; XP-C repair-complementing complex 58 kDa protein; p58

Dilution WB~~Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/20000. Not yet tested in other applications.

Format Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Storage Conditions -20℃

Rad23B Polyclonal Antibody - Protein Information

Name RAD23B

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

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in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase Rad23B Polyclonal Antibody - Background and delivering deglycosylated proteins to the proteasome. The XPC complex is Multiubiquitin chain receptor involved in proposed to represent the first factor bound modulation of proteasomal degradation. Binds at the sites of DNA damage and together to polyubiquitin chains. Proposed to be capable with other core recognition factors, XPA, to bind simultaneously to the 26S proteasome RPA and the TFIIH complex, is part of the and to polyubiquitinated substrates and to pre-incision (or initial recognition) complex. deliver ubiquitinated proteins to the The XPC complex recognizes a wide proteasome. May play a role in endoplasmic spectrum of damaged DNA characterized by reticulum- associated degradation (ERAD) of distortions of the DNA helix such as misfolded glycoproteins by association with single-stranded loops, mismatched bubbles PNGase and delivering deglycosylated proteins or single-stranded overhangs. The to the proteasome. The XPC complex is orientation of XPC complex binding appears proposed to represent the first factor bound at to be crucial for inducing a productive NER. the sites of DNA damage and together with XPC complex is proposed to recognize and other core recognition factors, XPA, RPA and to interact with unpaired bases on the the TFIIH complex, is part of the pre-incision undamaged DNA strand which is followed (or initial recognition) complex. The XPC by recruitment of the TFIIH complex and complex recognizes a wide spectrum of subsequent scanning for lesions in the damaged DNA characterized by distortions of opposite strand in a 5'-to-3' direction by the the DNA helix such as single-stranded loops, NER machinery. Cyclobutane pyrimidine mismatched bubbles or single-stranded dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection overhangs. The orientation of XPC complex by the XPC complex due to a low degree of binding appears to be crucial for inducing a structural perurbation. Instead they are productive NER. XPC complex is proposed to detected by the UV-DDB complex which in recognize and to interact with unpaired bases turn recruits and cooperates with the XPC on the undamaged DNA strand which is complex in the respective DNA repair. In followed by recruitment of the TFIIH complex vitro, the XPC:RAD23B dimer is sufficient to and subsequent scanning for lesions in the initiate NER; it preferentially binds to opposite strand in a 5'-to-3' direction by the cisplatin and UV-damaged double-stranded NER machinery. Cyclobutane pyrimidine DNA and also binds to a variety of dimers (CPDs) which are formed upon chemically and structurally diverse DNA UV-induced DNA damage esacpe detection by adducts. XPC:RAD23B contacts DNA both 5' the XPC complex due to a low degree of and 3' of a cisplatin lesion with a preference structural perurbation. Instead they are for the 5' side. XPC:RAD23B induces a bend detected by the UV-DDB complex which in turn in DNA upon binding. XPC:RAD23B recruits and cooperates with the XPC complex stimulates the activity of DNA glycosylases in the respective DNA repair. In vitro, the TDG and SMUG1. XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and Cellular Location UV-damaged double-stranded DNA and also Nucleus. Cytoplasm. Note=The intracellular binds to a variety of chemically and distribution is cell cycle dependent. structurally diverse DNA adducts. XPC:RAD23B Localized to the nucleus and the cytoplasm contacts DNA both 5' and 3' of a cisplatin during G1 phase. Nuclear levels decrease lesion with a preference for the 5' side. during S-phase; upon entering mitosis, XPC:RAD23B induces a bend in DNA upon relocalizes in the cytoplasm without association with chromatin binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.

Rad23B Polyclonal Antibody - Protocols

Provided below are standard protocols that you may find useful for product applications.

Page 2/3 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609

• Western Blot • Blocking Peptides • Dot Blot • Immunohistochemistry • Immunofluorescence • Immunoprecipitation • Flow Cytomety • Cell Culture

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