Key features and details
- Expression system: Wheat germ
- Suitable for: WB, SDS-PAGE, ELISA
Product nameRecombinant Human hHR23A protein
Expression systemWheat germ
Protein lengthFull length protein
SequenceMAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIY AGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESS TSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGRE EDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLT GIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQ NPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGE VGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENL AANFLLSQNFDDE
Predicted molecular weight66 kDa including tags
Amino acids1 to 363
Our Abpromise guarantee covers the use of ab152648 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
- hHR 23A
FunctionMultiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked 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.
Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.
Involved in vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome.
Sequence similaritiesBelongs to the RAD23 family.
Contains 2 UBA domains.
Contains 1 ubiquitin-like domain.
DomainThe ubiquitin-like domain mediates interaction with ATXN3.
The ubiquitin-like (UBL) and the UBA (ubiquitin-associated) domains interact intramolecularly in a highly dynamic manner, as each UBA domain competes for an overlapping UBL domain surface. Binding of ubiquitin or proteasome subunit PSMD4 disrupt the UBL-UBA domain interactions and drive RAD23A in to an open conformation.
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab152648 has not yet been referenced specifically in any publications.