HSPA6 Full-Length MS Protein Standard

heat shock 70kDa protein 6 (HSP70B′)

HSPA6 Full-Length MS Protein Standard (NP_002146), Labeled with [U- ¹³C₆, ¹⁵N₄]-L-Arginine and [U- ¹³C₆, ¹⁵N₂]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. 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.

HSPA6

heat shock 70kD protein 6 (HSP70B); heat shock 70kDa protein 6 (HSP70B)

NM_002155

1q23

[U- ¹³C₆, ¹⁵N₄]-L-Arg and [U- ¹³C₆, ¹⁵N₂]-L-Lys

> 80% as determined by SDS-PAGE and Coomassie blue staining

Human HEK293 cells

70.8 kDa

RC207795

>RC207795 representing NM_002155
MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVF
DAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQP
VKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVS
VLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSST
QATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQK
LLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNA
TIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSV
TATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESL
RDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQ
GDPSTGPIIEEVD