RAD23 Homolog B (S. Cerevisiae) (RAD23B) antibody

Antigen: RAD23 Homolog B (S. Cerevisiae) (RAD23B)

Synonyms: P58, HR23B, HHR23B, p58, mHR23B, AV001138, 0610007D13Rik, MGC112630, MGC137555, RAD23B, MGC107846

Clonality: Polyclonal

Host: Goat

Reactivity: Human, Mouse (Murine), Rat (Rattus), Sheep (Ovine)

Application: ELISA, Western Blotting (WB), Immunoprecipitation (IP)

Catalog no.: ABIN129561

Additional Information

Alternative name: HHR23B (RAD23B)

Gene ID: NP_002865

Swiss-Prot: P54727

Immunogen: This affinity purified antibody was prepared from whole goat serum produced by repeated immunizations with asynthetic peptide corresponding aa 163-176 of human HR23B protein.

Format: Liquid (sterile filtered)

Description: HR23B (also knownas UV excision repair protein RAD23 homologB, XP-C repair complementing complex 58 kDaprotein and p58) is one of two human homologsof Saccharomyces cerevisiae Rad23 (hHR23Aand hHR23B), a protein involved in nucleotideexcision repair (NER). This protein was shownto interact with, and elevate the nucleotideexcision activity of 3-methyladenine-DNAglycosylase (MPG), which suggested a role inDNA damage recognition in base excisionrepair. This protein contains an N-terminalubiquitin-like domain, which was reported tointeract with 26S proteasome, as well as withubiquitin protein ligase E6AP, and thus suggeststhat this protein may be involved in the ubiquitinmediated proteolytic pathway in cells.

Specificity: This is an affinity-purified antibody produced by immunoaffinity chromatography using the immunizingpeptide after immobilization to a solid phase. Reactivity occurs against human HR23B protein. Sequence homology asassessed by BLAST indicated 100% homology for this protein from human, dog, chimpanzee and S. cerevisiae. Crossreactivity with HR23B protein from mouse and rat may also occur as sequence homology varies by one amino acid residue inthis sequence by BLAST analysis. Reactivity with HR23B protein from other sources is not known.

Application Details

Application Notes: This affinity purified antibody has been tested for use in ELISA and by western blot. Specific conditionsfor reactivity should be optimized by the end user. Expect a band approximately 58 kDa in size corresponding to HR23B bywestern blotting in the appropriate cell lysate or extract. Dilutions: ELISA 1:2,000 - 1:10,000 WESTERN BLOT 1:500 - 1:2,000 IF MICROSCOPY User Optimized OTHER APPLICATIONS User Optimized

Concentration: 1.1 mg/ml (by UV absorbance at 280 nm)

Buffer: Stabilizer: None. Preservative: 0.01% (w/v) Sodium Azide. Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2.

Storage: Store vial at -20° C prior to opening. Dilute only prior to immediate use. For extended storage aliquotcontents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date ofopening.

Restrictions: For Research Use only

Images

Western blot using antibodies-online's affinity purified anti- HR23B antibody shows detection of a band at ~58 kDa (arrowhead) corresponding to HR23B present in a HeLa whole cell lysate. Pre-incubation of antibody with immunizing peptide completely blocks reactivity (data not shown). Approximately 33 ug of lysate was separated by 4-20% Tris Glycine SDS-PAGE. After blocking the membrane was probed overnight at 4

Role of HR23B in nucleotide excision repair (NER). NER mechanism recognizes damaged DNA regions based on their abnormal structure as well as on their abnormal chemistry, then excises and replaces them. The overall process of NER in eukaryotic cells resembles that in E. coli. The initial steps depend on whether the damage is in the actively transcribed strand of a gene or elsewhere in the genome. If the damage is not in the actively transcribed strand of a gene, then the damage is recognized and bound by a heterodimer consisting of the XPC and HR23B proteins. The binding of XPC and HR23B initiates the process of global genome repair (GGR). The XPC/HR23B dimer appears to recognize damaged DNA based on the extent of distortion of the normal helical DNA structure caused by the damage. In the process of binding to the damaged region, XPC/HR23B is thought to further increase the extent of structural distortion.

Publications

Publications: Shen, Valencia, Szostak et al.: "Scanning the human proteome for calmodulin-binding proteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 17, pp. 5969-74, 2005 (PubMed).

Crosby, Kulshreshtha, Ivan et al.: "MicroRNA regulation of DNA repair gene expression in hypoxic stress." in: Cancer research, Vol. 69, Issue 3, pp. 1221-9, 2009 (PubMed).