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Human Polyclonal RAD23B Primary Antibody for WB - ABIN2801856
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 1994
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Human Monoclonal RAD23B Primary Antibody for WB - ABIN1944896
Huang, Wang, Xu, Lu, Xu, Li, Zhou, Sha: Expression of a novel RAD23B mRNA splice variant in the human testis. in Journal of andrology 2004
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Human Polyclonal RAD23B Primary Antibody for ELISA, WB - ABIN129561
Shen, Valencia, Szostak, Szostak, Dong, Liu: Scanning the human proteome for calmodulin-binding proteins. in Proceedings of the National Academy of Sciences of the United States of America 2005
Show all 2 Pubmed References
Human Polyclonal RAD23B Primary Antibody for ICC, IF - ABIN4317293
Jones, Moskaluk, Gillenwater, Petroni, Burks, Philips, Rehm, Olazagasti, Kozower, Bao: Phase I trial of induction histone deacetylase and proteasome inhibition followed by surgery in non-small-cell lung cancer. in Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer 2012
miR-196b improved radiosensitivity of SNU-638 cells by targeting RAD23B.
Several mutations in the two parts of the central "crest" of the arrestin molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 interactions with several GPCRs in receptor subtype and functional state-specific manner.
XPC dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER) of certain types of DNA adducts, leading to repression of NER.
HR23B role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]
Data show that nucleotide excision repair factor XPC-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1).
Data indicate that phosphorylation provides a mechanism to regulate Rad23/proteasome interaction.
RAD23B has a potential role in breast cancer progression and a tumor suppressor role of nuclear RAD23B in breast cancer.
It is unlikely that the RAD23B 249Val/Val polymorphism may contribute to the individual susceptibility to cancer risk.
Results define a regulatory mechanism that involves the interplay between HR23B and HDAC6 that influences the biological outcome of HDAC inhibitor treatment.
Polymorphism in RAD23B gene is associated with breast cancer.
HR23B expression was associated with disease stabilization for patients with unresectable hepatocellular carcinoma treated with epigenetic therapy using belinostat, a histone deacetylase inhibitor.
Single nucleotide polymorphisms of CCND2, RAD23B, GRP78, CEP164, MDM2, and ALDH2 genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
PNGase-PUB serves not only as p97-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
26S proteasomes and p97/VCP complexes bind to the ubiquitin-like domain of HHR23B.
Gene expression of RAD23B was down-regulated during early apoptosis in human hepatoma cells exposed to Paeoniae Radix extract in vitro.
analysis of mHR23A/B double-mutant cells showed that HR23 proteins function in nucleotide excision repair by governing xeroderma pigmentosum group C protein stability via partial protection against proteasomal degradation
structure of the ubiquitin-interacting motif of the proteasome subunit S5a bound to the ubiquitin-like domain of HR23B
hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation
Highly expressed in the human testis and in ejaculated spermatozoa. This novel alternative splicing form of RAD23B is correlated with human spermatogenesis.
the human nucleotide excision repair gene, hHR23B, is epigenetically silenced in interleukin-6-responsive multiple myeloma KAS-6/1 cells
data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology.
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC to DNA damage in living cells in addition to stabilizing XPC. RAD23 proteins rapidly dissociated from XPC upon binding to damaged DNA.
The crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B is described; the results suggest a co-evolution of ER-associated degradation and DNA repair pathways.
This illustrates that impairment of the ubiquitin-proteasome system (UPS) by expanded glutamine repeats, including the sequestration of HR23B, is not affecting NER.
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER). This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
RAD23, yeast homolog of, B
, UV excision repair protein RAD23 homolog B
, XP-C repair complementing complex 58 kDa
, XP-C repair complementing protein
, XP-C repair-complementing complex 58 kDa protein
, RAD23b homolog
, RAD23 homolog B (S. cerevisiae)
, RAD23 homolog B