- CITATIONS: 2
|Application ||WB, IHC-P, IF, FC, E|
|Calculated MW||72333 Da|
|Other Names||78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78|
|Target/Specificity||This HSPA5 antibody is generated from rabbits immunized with a recombinant protein encoding full length human HSPA5.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSPA5 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.|
|Cellular Location||Endoplasmic reticulum lumen. Melanosome. Cytoplasm Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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. The HSP70s in mitochondria and the endoplasmic reticulum play an additional role by providing a driving force for protein translocation. They are involved in signal transduction pathways in cooperation with HSP90. They 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.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002). Milner, C.M., et al., Immunogenetics 32(4):242-251 (1990). Sargent, C.A., et al., Proc. Natl. Acad. Sci. U.S.A. 86(6):1968-1972 (1989). Drabent, B., et al., Nucleic Acids Res. 14(22):8933-8948 (1986). Hunt, C., et al., Proc. Natl. Acad. Sci. U.S.A. 82(19):6455-6459 (1985).
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