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G4170

Sigma-Aldrich

Anti-GRP75 (KA-20) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Glucose Regulated Protein 75, Anti-HSP70-9B, Anti-Mitochondrial Hsp70, Anti-Mortalin, Anti-Peptide Binding Protein 74 (PBP74)

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About This Item

MDL number:
MFCD00164609
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 75 kDa

species reactivity

canine, rat, human, mouse

concentration

~1 mg/mL

technique(s)

microarray: suitable
western blot: 0.2-0.4 μg/mL using mouse fibroblasts NIH3T3, human HeLa, and Madin Darby canine kidney cells

UniProt accession no.

P38646

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HSPA9(3313)
mouse ... Hspa9(15526)

General description

GRPs are unresponsive to heat stress and are induced by stress related to glucose starvation or defects in glycoprotein processing. GRP75/mortalin has been localized mainly to the endoplasmic reticulum (ER), but also to various cellular compartments including mitochondria and cytoplasmic vesicles.

Immunogen

synthetic peptide corresponding to amino acids 617-636 located near the C-terminus of human GRP75/mortalin-2. This sequence is identical in rat GRP75 and highly conserved in chicken (1 amino acid substitution) and mouse (2 amino acids substitutions) GRP75.

Application

Anti-GRP75 antibody produced in rabbit is suitable for microarray and immunoblotting at a working antibody concentration of 0.2-0.4μg/mL using whole cell extracts of the human epitheloid carcinoma HeLa cells, Madin-Darby canine kidney (MDCK) cells, and mouse fibroblasts NIH3T3 cells.

Biochem/physiol Actions

GRP75 (glucose-regulated protein 75) belongs to a subfamily of the heat shock proteins Hsp70. It is involved in stress responses to intracellular trafficking, antigen processing, and control of cell proliferation, differentiation, and tumorigenesis. It is induced by low levels of ionizing radiation, glucose deprivation, calcium ionophore, and ozone and its levels correlate with muscle activity, mitochondrial activity, and biogenesis.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Certificates of Analysis (COA)

Lot/Batch Number
055K4813

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Q Ran et al.
Biochemical and biophysical research communications, 275(1), 174-179 (2000-08-17)
Subcellular fractionation and immunofluorescence microscopy were used to identify the specific sites of intracellular residence of mortalin, also called a mitochondrial homologue of the hsp70 family, in immortal human cell lines previously assigned to four distinct complementation groups (A-D) for
Renu Wadhwa et al.
Cell stress & chaperones, 7(3), 309-316 (2002-12-17)
Mortalin/mthsp70/PBP74/Grp75 (called mortalin hereafter), a member of the Hsp70 family of chaperones, was shown to have different subcellular localizations in normal and immortal cells. It has been assigned to multiple subcellular sites and implicated in multiple functions ranging from stress
T Bhattacharyya et al.
The Journal of biological chemistry, 270(4), 1705-1710 (1995-01-27)
We report the cloning, nucleotide sequence, and localization of mitochondrial hsp70, a member of the human hsp70 multi-gene family. The human mthsp75 gene was cloned by screening an expression library with monoclonal antibody 3A3 that recognizes three members of the
A S Lee
Trends in biochemical sciences, 26(8), 504-510 (2001-08-16)
A protective mechanism used by cells to adapt to stress of the endoplasmic reticulum (ER) is the induction of members of the glucose-regulated protein (Grp) family. The induction of mammalian Grp proteins in response to ER stress involves a complex
R Wadhwa et al.
The Journal of biological chemistry, 268(30), 22239-22242 (1993-10-25)
We have recently identified a novel member of hsp70 family (mortalin) as a mortality marker (Wadhwa, R., Kaul, S. C., Ikawa, Y., and Sugimoto, Y. (1993) J. Biol. Chem. 268, 6615-6621). It has distinct intracellular distribution in mortal and immortal

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