Recombinant Human Uv Excision Repair Protein Rad23 Homolog A (RAD23A) Protein (His&Myc)

Name: Recombinant Human Uv Excision Repair Protein Rad23 Homolog A (RAD23A) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07603P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Uv Excision Repair Protein Rad23 Homolog A (RAD23A) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P54725
Target Symbol	RAD23A
Synonyms	(HR23A)(hHR23A)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPATSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
Expression Range	1-362aa(T131A)
Protein Length	Full Length of Isoform 3
Mol. Weight	47.0 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.; 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.; (Microbial infection) 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.
Subcellular Location	Nucleus.
Protein Families	RAD23 family
Database References	HGNC: 9812 OMIM: 600061 KEGG: hsa:5886 STRING: 9606.ENSP00000467024 UniGene: Hs.643267

Gene Functions References

Data indicate that HR23A protein-depleted cells exhibit enhanced autophagy when treated with DNA-damaging agents. PMID: 27613096
HR23A role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review] PMID: 27771451
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
Data indicate that phosphorylation provides a mechanism to regulate Rad23/proteasome interaction. PMID: 25311859
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
this study identified RAD23A as a novel negative regulator of RIG-I/MDA5 mediated anti-virus response. PMID: 23357418
Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography. PMID: 21047872
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
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
structures of the UBA domains of HHR23A reveal a conserved hydrophobic surface for protein-protein interactions PMID: 12079361
the solution structures of the HHR23A Ubl domain PMID: 12970176
Adopts a closed conformation and binds to the proteasomal subunit S5a thereby changing its own conformation. PMID: 14557549
hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation PMID: 14645509
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
hHR23A regulates the function of xeroderma pigmentosum C by its association with the nucleotide excision repair activator p53 PMID: 16105547
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
hHR23B thus plays a critical role in the activation and function of p53 after specific genotoxic exposures. PMID: 16924240
hHR23a and hPLIC2 interact via UBL/UBA domain interactions PMID: 17098253
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.