Recombinant Human UV excision repair protein RAD23 homolog A(RAD23A)

Code CSB-YP019259HU
Size US$2010
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names RAD23A
Uniprot No. P54725
Research Area Epigenetics and Nuclear Signaling
Alternative Names hHR 23A; hHR23A; HR23A; MGC111083; RAD 23a; RAD23 homolog A (S. cerevisiae); RAD23 homolog A; RAD23 yeast homolog A; RAD23A; RD23A_HUMAN; UV excision repair protein RAD23; UV excision repair protein RAD23 homolog A
Species Homo sapiens (Human)
Source Yeast
Expression Region 1-363aa
Target Protein Sequence MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 41.6kDa
Protein Length Full Length
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Multiubiquitin 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.; FUNCTION
Gene References into Functions
  1. Data indicate that HR23A protein-depleted cells exhibit enhanced autophagy when treated with DNA-damaging agents. PMID: 27613096
  2. HR23A role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review] PMID: 27771451
  3. hHR23A associates with Chk1 through its ubiquitin-associated domains, and knockdown of hHR23A increases and stabilizes the protein level of Chk1 and its phosphorylation at S347. PMID: 26296656
  4. Data indicate that phosphorylation provides a mechanism to regulate Rad23/proteasome interaction. PMID: 25311859
  5. Here, we show that hHR23A utilizes both the UBA2 and XPCB domains to form a stable complex with Vpr, linking Vpr directly to cellular DNA repair pathways and their probable exploitation by the virus. PMID: 24318982
  6. this study identified RAD23A as a novel negative regulator of RIG-I/MDA5 mediated anti-virus response. PMID: 23357418
  7. Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography. PMID: 21047872
  8. Vpr promotes hHR23A-mediated protein-ubiquitination, and down-regulation of hHR23A using RNAi significantly reduced viral replication in non-proliferating MAGI-CCR5 cells and primary macrophages PMID: 20614012
  9. involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination PMID: 11788722
  10. structures of the UBA domains of HHR23A reveal a conserved hydrophobic surface for protein-protein interactions PMID: 12079361
  11. the solution structures of the HHR23A Ubl domain PMID: 12970176
  12. Adopts a closed conformation and binds to the proteasomal subunit S5a thereby changing its own conformation. PMID: 14557549
  13. hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation PMID: 14645509
  14. Data suggest that the UBL domain of HHR23A negatively regulates polyubiquitin/UBA interactions and identify leucine 8 of ubiquitin as an important determinant of chain recognition. PMID: 15321727
  15. hHR23A regulates the function of xeroderma pigmentosum C by its association with the nucleotide excision repair activator p53 PMID: 16105547
  16. Ufd4, the E3 component of the UFD pathway, is involved in controlling the degradation of Rad4, and Ufd4 and Rad23 exhibit a synthetic inhibitory effect on Rad4 degradation PMID: 16430867
  17. hHR23B thus plays a critical role in the activation and function of p53 after specific genotoxic exposures. PMID: 16924240
  18. hHR23a and hPLIC2 interact via UBL/UBA domain interactions PMID: 17098253
  19. Pyramidal crystals of the UbL domain of hHR23A were diffracted to beyond 2 A resolution and the structure was solved by molecular replacement. PMID: 19724136

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Subcellular Location Nucleus
Protein Families RAD23 family
Database Links

HGNC: 9812

OMIM: 600061

KEGG: hsa:5886

STRING: 9606.ENSP00000467024

UniGene: Hs.643267

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