Heat shock protein 82 (HSP82), Recombinant Protein
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Heat shock protein 82 (HSP82), Recombinant Protein

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Cat: RP17711
Size: 0.02 mg (E-Coli)/ 0.02 mg (Yeast)/ 0.1 mg (E-Coli)/ 0.1 mg (Yeast)/ 0.02 mg (Baculovirus)/ 0.02 mg (Mammalian-Cell)/ 0.1 mg (Baculovirus)/ 1 mg (E-Coli)/ 1 mg (Yeast)/ 0.1 mg (Mammalian-Cell)/ 1 mg (Baculovirus)/ 0.5 mg (Mammalian-Cell)
Species: Nicotiana tabacum (Common tobacco)
Datasheet:

Product Info

Full Product Name
Recombinant Nicotiana tabacum Heat shock protein 82 (HSP82)
Product Gene Name
HSP82 recombinant protein
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Sequence
EFISYPIYLW TEKTTEKEIS DDEDDEPKKD EEGAVEEVDE DKEKEKGKKK KIKEVSHEWQ LINKQKPIWL RKPEEITKDE YASFYKSLTN DWEEHLAVKH FSVEGQLEFK AILFVPKRAP FDLFDTRKKM NNIKLYVRRV FIMDNCEELI PEYLGFVKGV VDSDDLPLNI SREMLQQNKI LKVIRKNLVK KCIEMFNEIA ENKEDYNKFY EAFSKNLKLG IHEDSQNRAK LADLLRYHST KSGDEMTSLK DYVTRMKEGQ KDIYYITGES KKAVENSPFL ERLKKKGYEV LYMVDAIDEY AVGQLKEYDG KKLVSATKEG LKLDDDSEEE KKKKEEKKKS FENLCKIIKD ILGDKVEKVV VSDRIVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMSSY MSSKKTMEIN PDNGIMEELR KRAEADKNDK SVKDLVLLLF ETALLTSGFS LDDPNTFAAR IHRMLKLGLS IDEEEEAVED ADMPALEETG EESKMEEVD
Sequence Positions
1-499, Full length protein
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
58,021 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
Heat shock protein

NCBI/Uniprot Data

NCBI Accession #
P36182.1
NCBI GI #
547684
NCBI Official Full Name
Heat shock protein 82
UniProt Gene Name
HSP82  
UniProt Protein Name
Heat shock protein 82
UniProt Primary Accession #
P36182
UniProt Comments
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.

For research use only, not for clinical use.