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Dog (Canine) Monoclonal RAD23B Primary Antibody für IF, WB - ABIN968320
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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Dog (Canine) Monoclonal RAD23B Primary Antibody für IF, WB - ABIN968319
Reardon, Mu, Sancar: Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease. in The Journal of biological chemistry 1996
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Human Polyclonal RAD23B Primary Antibody für WB - ABIN2801856
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 Monoclonal RAD23B Primary Antibody für WB - ABIN1944896
Ota, Suzuki, Nishikawa, Otsuki, Sugiyama, Irie, Wakamatsu, Hayashi, Sato, Nagai, Kimura, Makita, Sekine, Obayashi, Nishi, Shibahara, Tanaka, Ishii, Yamamoto, Saito, Kawai, Isono, Nakamura, Nagahari et al.: Complete sequencing and characterization of 21,243 full-length human cDNAs. ... in Nature genetics 2003
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Human Polyclonal RAD23B Primary Antibody für 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
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Human Polyclonal RAD23B Primary Antibody für 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
Several mutations in the two parts of the central "crest" of the arrestin (zeige SAG Antikörper) molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 (zeige ARRB2 Antikörper) interactions with several GPCRs in receptor subtype and functional state-specific manner.
XPC (zeige XPC Antikörper) dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER (zeige NR1H2 Antikörper)) of certain types of DNA adducts, leading to repression of NER (zeige NR1H2 Antikörper).
HR23B role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]
Data show that nucleotide excision repair factor XPC (zeige XPC Antikörper)-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1 (zeige PARP1 Antikörper)).
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 (zeige HDAC6 Antikörper) that influences the biological outcome of HDAC (zeige HDAC3 Antikörper) 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 (zeige HDAC1 Antikörper) inhibitor.
Single nucleotide polymorphisms of CCND2 (zeige CCND2 Antikörper), RAD23B, GRP78 (zeige HSPA5 Antikörper), CEP164 (zeige CEP164 Antikörper), MDM2 (zeige MDM2 Antikörper), and ALDH2 (zeige ALDH2 Antikörper) 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 (zeige XPC Antikörper) to DNA damage in living cells in addition to stabilizing XPC (zeige XPC Antikörper). RAD23 proteins rapidly dissociated from XPC (zeige XPC Antikörper) 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 (zeige GFPT1 Antikörper) repeats, including the sequestration of HR23B, is not affecting NER (zeige NR1H2 Antikörper).
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.
UV excision repair protein RAD23 homolog B
, RAD23 homolog B (S. cerevisiae)
, RAD23 homolog B
, RAD23, yeast homolog of, B
, XP-C repair complementing complex 58 kDa
, XP-C repair complementing protein
, XP-C repair-complementing complex 58 kDa protein
, RAD23b homolog