Coiled-coil domain-containing protein 39 (CCDC39) Recombinant Protein | CCDC39 recombinant protein

Recombinant Chlamydomonas reinhardtii Coiled-coil domain-containing protein 39 (CCDC39), partial

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Coiled-coil domain-containing protein 39 (CCDC39); Recombinant Chlamydomonas reinhardtii Coiled-coil domain-containing protein 39 (CCDC39); partial; CCDC39 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 Length: 894

• Species: Chlamydomonas reinhardtii (Chlamydomonas smithii)
• 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.

NCBI and Uniprot Product Information

• NCBI GI #: 159467164
• NCBI GeneID: 5717298
• NCBI Accession #: XP_001691768.1
• NCBI GenBank Nucleotide #: XM_001691716.1
• UniProt Accession #: A8IQE0
• Molecular Weight: 101,488 Da
• NCBI Official Full Name: flagellar associated protein
• NCBI Official Symbol: FAP59
• NCBI Protein Information: flagellar associated protein
• UniProt Protein Name: Coiled-coil domain-containing protein 39
• Protein Family: Coiled-coil domain-containing protein
• UniProt Gene Name: CCDC39

Uniprot Description

Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (PubMed:25395538). Together with CCDC40/FAP172 forms a 96-nm-long complex in flagella. This complex does not act as a physical ruler, but rather act as a negative regulator for radial spokes: the complex lays along specific protofilaments, masking radial spoke binding sites and allowing recruitment of inner dynein arm (IDA) and nexin-dynein regulatory complexes (N-DRC) (PubMed:25395538).