Recombinant Human UV excision repair protein RAD23 homolog A (RAD23A) | CSB-EP019259HU

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CSB-EP019259HU
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  • Recombinant Human UV excision repair protein RAD23 homolog A (RAD23A)
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
$294.00 - $1,532.40

Description

Recombinant Human UV excision repair protein RAD23 homolog A (RAD23A) | CSB-EP019259HU | Cusabio

Alternative Name(s): 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

Gene Names: RAD23A

Research Areas: Epigenetics and Nuclear Signaling

Organism: Homo sapiens (Human)

AA Sequence: MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE

Source: E.coli

Tag Info: N-terminal GST-tagged

Expression Region: 1-363aa

Sequence Info: Full Length

MW: 66.6 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Relevance: 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.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.

Reference: Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins.Goh A.M., Walters K.J., Elsasser S., Verma R., Deshaies R.J., Finley D., Howley P.M.BMC Biochem. 9:4-4(2008)

Storage: 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?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.

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

Involvement in disease:

Subcellular Location: Nucleus

Protein Families: RAD23 family

Tissue Specificity:

Paythway: Proteinprocessinginendoplasmicreticulum

Form: Liquid or Lyophilized powder

Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. 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?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Uniprot ID: P54725

HGNC Database Link: HGNC

UniGene Database Link: UniGene

KEGG Database Link: KEGG

STRING Database Link: STRING

OMIM Database Link: OMIM

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