|Application ||WB, ICC|
|Calculated MW||70 KDa|
|Other Names||DAQB 147D11.1 001;FLJ54303;FLJ54370;FLJ54392;FLJ54408;FLJ75127;Heat shock 70 kDa protein 1;Heat shock 70 kDa protein 1/2;Heat shock 70 kDa protein 1A/1B;heat shock 70kDa protein 1A;Heat shock 70kDa protein 1B;Heat shock induced protein;heat shock protein 70;HSP70 1; HSP70 2;HSP70-1/HSP70-2;HSP70-1A;HSP70.1;HSP70.1/HSP70.2;HSP70I;HSP71_HUMAN;HSP72; HSPA1;HSPA1A;HSPA1B;XXbac BCX40G17.3 001.|
|Format||Purified mouse monoclonal in buffer containing 0.1M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.02% sodium azide, 50%,glycerol|
|Storage||Store at -20 °C.Stable for 12 months from date of receipt|
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Provided below are standard protocols that you may find useful for product applications.
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. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
Milner C.M.,et al.Immunogenetics 32:242-251(1990).
Hunt C.,et al.Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985).
Xie T.,et al.Genome Res. 13:2621-2636(2003).
Shiina S.,et al.Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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