Product namehHR23b overexpression 293T lysate (whole cell)
See all hHR23b lysates
ab94298 is a 293T cell transfected lysate in which Human hHR23b has been transiently over-expressed using a pCMV-hHR23b plasmid. The lysate is provided in 1 x Sample Buffer. Note: For more details about how the transfected lysate was prepared view preparation notes
Tested applicationsSuitable for: WBmore details
Storage instructionsShipped on dry ice. Upon delivery aliquot and store at -20ºC. Avoid freeze / thaw cycles.
Storage bufferConstituents: 0.01% Bromophenol blue, 2.3% Beta mercaptoethanol, 2% Sodium lauryl sulfate, 0.788% Tris HCl, 10% Glycerol (glycerin, glycerine)
Concentration information loading...
BackgroundFunction: 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 in endoplasmatic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1. Similarity: Belongs to the RAD23 family. Contains 1 STI1 domain. Contains 2 UBA domains. Contains 1 ubiquitin-like domain. Domain: The ubiquitin-like domain mediates interaction with ATXN3.
Our Abpromise guarantee covers the use of ab94298 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use at an assay dependent dilution.|
ab94298 at 15µg/lane on an SDS-PAGE gel.
All lanes : Anti-hHR23b antibody (ab88503) at 1/500 dilution
Lane 1 :
hHR23b overexpression 293T lysate (whole cell) (ab94298)
Lane 2 : 293T non-transfected lysate
Lysates/proteins at 25 µg per lane.
All lanes : Goat Anti-mouse IgG (H and L) HRP conjugated at 1/2500 dilution
ab94298 has not yet been referenced specifically in any publications.