|Flow Cytometry (Flow)||1:10-1:50|
|Western Blot (WB)||1:1000|
|Western Blot (WB)||See 1 publications below|
|Tested Species reactivity||Human, Mouse|
|Published species reactivity||Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant protein encoding full length human HSPA5|
|Purification||Ammonium sulfate precipitation, Size-exclusion - Dialysis|
|Contains||0.09% sodium azide|
|Storage conditions||-20° C, Avoid Freeze/Thaw Cycles|
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: 78 kDa glucose-regulated protein; BiP; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; epididymis secretory sperm binding protein Li 89n; glucose regulated protein, 78 kDa; glucose-regulated protein, 78kDa; GRP-78; Heat Shock 70 kDa protein 5; heat shock 70kD protein 5 (glucose-regulated protein, 78kD); heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Immunoglobulin heavy chain-binding protein; XAP-1 antigen
Gene Aliases: AL022860; AU019543; baffled; BIP; D2Wsu141e; D2Wsu17e; GRP78; HEL-S-89n; Hsce70; HSPA5; mBiP; MIF2; SEZ-7; Sez7
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