Preprotein translocase subunit SCY1, chloroplastic (SCY1), Recombinant Protein
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Preprotein translocase subunit SCY1, chloroplastic (SCY1), Recombinant Protein

Cat: RP03529
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:

Product Info

Full Product Name
Recombinant Arabidopsis thaliana Preprotein translocase subunit SCY1, chloroplastic (SCY1), partial
Product Gene Name
SCY1 recombinant protein
Product Synonym Gene Name
SCY1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
59,492 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.
Protein Family
Preprotein translocase

NCBI/Uniprot Data

NCBI Accession #
NP_179461.1
NCBI GI #
15224214
NCBI GenBank Nucleotide #
NM_127427.3
NCBI GeneID
816386
NCBI Official Full Name
SECY homolog 1
NCBI Official Symbol
SCY1
NCBI Official Synonym Symbols
SECY homolog 1
NCBI Protein Information
SECY homolog 1
NCBI Summary
Encodes a component of the thylakoid-localized Sec system involved in the translocation of cytoplasmic proteins into plastid.
UniProt Gene Name
SCY1
UniProt Synonym Gene Names
SECY
UniProt Protein Name
Preprotein translocase subunit SCY1, chloroplastic
UniProt Synonym Protein Names
CpSecY
UniProt Primary Accession #
Q38885
UniProt Secondary Accession #
Q9SLG1
UniProt Related Accession #
Q38885
UniProt Comments
Involved in protein export. Probably interacts with other proteins to allow the translocation of proteins across the chloroplast thylakoid membranes. Required for normal greening during embryogenesis. Central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug .

For research use only, not for clinical use.