Outer envelope protein 61, chloroplastic (OEP61), Recombinant Protein
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Outer envelope protein 61, chloroplastic (OEP61), Recombinant Protein

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Cat: RP05372
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:

Product Info

Full Product Name
Recombinant Arabidopsis thaliana Outer envelope protein 61, chloroplastic (OEP61) , partial
Product Gene Name
OEP61 recombinant protein
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
60,757 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
Outer envelope protein

NCBI/Uniprot Data

NCBI Accession #
NP_680187.2
NCBI GI #
30688239
NCBI GenBank Nucleotide #
NM_147882.3
NCBI GeneID
832259
NCBI Official Full Name
Tetratricopeptide repeat (TPR)-like superfamily protein
NCBI Official Symbol
TPR7
NCBI Official Synonym Symbols
AtTPR7; OEP61; outer envelope protein 61; tetratricopeptide repeat 7
NCBI Protein Information
Tetratricopeptide repeat (TPR)-like superfamily protein
NCBI Summary
Encodes one of the 36 carboxylate clamp (CC)-tetratricopeptide repeat (TPR) proteins (Prasad 2010, Pubmed ID: 20856808). Functions as a chaperone receptor at the chloroplast outer envelope, mediating Hsp70-dependent protein targeting to chloroplasts. It has been localized to the ER membrane, interacts with the Sec translocon, and has a potential function in post-translational protein transport into the ER.
UniProt Gene Name
OEP61
UniProt Synonym Gene Names
TPR7
UniProt Protein Name
Outer envelope protein 61
UniProt Synonym Protein Names
Tetratricopeptide repeat domain-containing protein 7
UniProt Primary Accession #
B7ZWR6
UniProt Secondary Accession #
Q8GWM6; Q9C588
UniProt Related Accession #
B7ZWR6
UniProt Comments
Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post-translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70.

For research use only, not for clinical use.