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Human Monoclonal RAD23B Primary Antibody pour WB - ABIN1944896
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. dans The EMBO journal 1994
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Human Polyclonal RAD23B Primary Antibody pour WB - ABIN2801856
Huang, Wang, Xu, Lu, Xu, Li, Zhou, Sha: Expression of a novel RAD23B mRNA splice variant in the human testis. dans Journal of andrology 2004
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Human Polyclonal RAD23B Primary Antibody pour ELISA, WB - ABIN129561
Shen, Valencia, Szostak, Szostak, Dong, Liu: Scanning the human proteome for calmodulin-binding proteins. dans Proceedings of the National Academy of Sciences of the United States of America 2005
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Human Polyclonal RAD23B Primary Antibody pour 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. dans Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer 2012
Several mutations in the two parts of the central "crest" of the arrestin (Montrer SAG Anticorps) molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 (Montrer ARRB2 Anticorps) interactions with several GPCRs in receptor subtype and functional state-specific manner.
XPC (Montrer XPC Anticorps) dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER (Montrer NR1H2 Anticorps)) of certain types of DNA adducts, leading to repression of NER (Montrer NR1H2 Anticorps).
HR23B role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]
Data show that nucleotide excision repair factor XPC (Montrer XPC Anticorps)-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1 (Montrer PARP1 Anticorps)).
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 (Montrer HDAC6 Anticorps) that influences the biological outcome of HDAC (Montrer HDAC3 Anticorps) 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 (Montrer HDAC1 Anticorps) inhibitor.
Single nucleotide polymorphisms of CCND2 (Montrer CCND2 Anticorps), RAD23B, GRP78 (Montrer HSPA5 Anticorps), CEP164 (Montrer CEP164 Anticorps), MDM2 (Montrer MDM2 Anticorps), and ALDH2 (Montrer ALDH2 Anticorps) genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC (Montrer XPC Anticorps) to DNA damage in living cells in addition to stabilizing XPC (Montrer XPC Anticorps). RAD23 proteins rapidly dissociated from XPC (Montrer XPC Anticorps) upon binding to damaged DNA.
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
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 (Montrer GFPT1 Anticorps) repeats, including the sequestration of HR23B, is not affecting NER (Montrer NR1H2 Anticorps).
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