|Tested species reactivity||Bovine, Dog, Guinea pig, Hamster, Human, Mouse, Non-human primate, Sheep, Pig, Rabbit, Rat, Xenopus|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Grp75 isolated from human Molt4 cells.|
|Storage buffer||ascites diluted in PBS, pH 7.2, with 0.1mM PMSF, 50% glycerol|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunocytochemistry (ICC)||Assay dependent|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:5000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
MA1-91639 detects Grp75 from human, rat, bovine, canine, Xenopus laevis, mouse, guinea pig, hamster, monkey, porcine, rabbit, and ovine samples.
MA1-91639 has been successfully used in immunocytochemistry, immunohistochemistry, Western blot, and immunoprecipitation applications. Western blot detects a band ~75 kDa. A suggested positive control is HeLa cell lysate (heat shocked).
The MA1-91639 immunogen is Grp75 isolated from human Molt4 cells.
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. One class of stress proteins, termed the Hsp70 family, is comprised of multiple members, all of which bind ATPin vitro, but which are localized within different intracellular compartments. These include: i) Hsc70 (or constitutive form) present within the cytosol/nucleus; ii) Hsp70 (inducible form) present within the cytosol/nucleus/nucleolus; iii) the constitutive glucose-regulated 78 kDa (or BiP) protein present within the lumen of the endoplasmic reticulum; and iv) the constitutive glucose regulated 75 kDa protein present within the mitochondrial matrix. Members of the Hsp70 family are thought to function as molecular chaperones, assisting in the folding of other proteins in various intracellular compartments. Grp75 is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.