Heat shock 70 kDa protein 14 (HSP70-14), Recombinant Protein
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Heat shock 70 kDa protein 14 (HSP70-14), Recombinant Protein

Cat: RP08973
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:

Product Info

Full Product Name
Recombinant Arabidopsis thaliana Heat shock 70 kDa protein 14 (HSP70-14) , partial
Product Gene Name
HSP70-14 recombinant protein
Product Synonym Gene Name
HSP70-14
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
87,317 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.

NCBI/Uniprot Data

NCBI Accession #
NP_001031305.1
NCBI GI #
79321519
NCBI GenBank Nucleotide #
NM_001036228.2
NCBI GeneID
844333
NCBI Official Full Name
heat shock protein 91
NCBI Official Symbol
HSP91
NCBI Official Synonym Symbols
AtHsp70-14; F19K16.11; F19K16_11; heat shock protein 91
NCBI Protein Information
heat shock protein 91
NCBI Summary
encodes high molecular weight heat shock protein 70 not a HSP90 homolog, mRNA is constitutively expressed but transiently induced after heat shock
UniProt Gene Name
HSP70-14
UniProt Synonym Gene Names
HSP91; AtHsp70-14
UniProt Protein Name
Heat shock 70 kDa protein 14
UniProt Synonym Protein Names
Heat shock protein 70-14; AtHsp70-14; Heat shock protein 91
UniProt Primary Accession #
Q9S7C0
UniProt Secondary Accession #
Q0WVB9; Q96269
UniProt Related Accession #
Q9S7C0
UniProt Comments
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage .

For research use only, not for clinical use.