Proteasome subunit alpha type-7 (Psma7) Recombinant Protein | Psma7 recombinant protein

Recombinant Rat Proteasome subunit alpha type-7 (Psma7)

Cat. Num. AAA963863

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Proteasome subunit alpha type-7 (Psma7); Recombinant Rat Proteasome subunit alpha type-7 (Psma7); Psma7 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-254, Full length protein
• Sequence: MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAVVASVSGLTADARIVINRARVECQSHRLTVGDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQPLKILSPEEIEKYVAEIEKEKEENEKKKQKKAS
• Sequence Length: 254

• Species: Rat
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Related Product Information for Psma7 recombinant protein

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP
ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.

NCBI and Uniprot Product Information

• NCBI GI #: 1346784
• NCBI GeneID: 29674
• UniProt Accession #: P48004
• Molecular Weight: 27,784 Da
• NCBI Official Full Name: Proteasome subunit alpha type-7
• NCBI Official Synonym Full Names: proteasome subunit alpha 7
• NCBI Official Symbol: Psma7
• NCBI Protein Information: proteasome subunit alpha type-7
• UniProt Protein Name: Proteasome subunit alpha type-7
• Protein Family: Proteasome
• UniProt Gene Name: Psma7

NCBI Description

human homolog may facilitate internal ribosome entry site mediated translation and replication of hepatitis C virus [RGD, Feb 2006]

Uniprot Description

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.