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Key Documents

G9043

Sigma-Aldrich

Anti-GRP78/BiP (ET-21) antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-78-kDa Glucose-Regulating Protein, Anti-Immunoglobulin Heavy Chain Binding Protein

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About This Item

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 78 kDa

species reactivity

mouse, chicken, Xenopus, hamster, human, rat

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunocytochemistry: 1:1,000 using methanol/acetone fixed cultured mouse fibroblast NIH3T3 cell line
immunohistochemistry: 1:1,000 using human cerebral cortex and human thyroid gland tissue sections
western blot: 1:3,000 using whole cell extract of human epitheloid carcinoma HeLa cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HSPA5(3309)
mouse ... Hspa5(14828)
rat ... Hspa5(25617)

Application

Anti-GRP78/BiP (ET-21) antibody produced in rabbit is suitable for use as a primary antibody:
  • for immunofluorescence staining of frozen heart tissue to examine whether ER stress signaling activation occurs in cardiomyocytes
  • for immunohistochemistry on Paraffin embedded sections of human cerebral cortex and human thyroid gland tissue sections.
  • to detect Bip by immunoblotting of protein extract from WT AB strain of zebrafish (Danio rerio)
  • at a working dilution of 1:1000 to detect GRP78 in extract of prostate cancer cells after androgen deprivation therapy
It is also suitable for immunoblotting at a working dilution of 1:3000 using human epitheloid carcinoma HeLa whole cell extract and for immunocytochemistry at a working dilution of 1:1000 using mouse fibroblasts NIH3T3 cells.

Biochem/physiol Actions

GRP78/BiP levels are elevated in Alzheimer′s disease brains and the decreased expression of GRP78/BiP is found associated with missense mutations in presenilin-1 (PS-1).
The GRP78 (78-kDa glucose-regulated protein) is a member of the heat shock proteins Hsp70 required for cell viability. It is a Ca2+-binding molecular chaperone that is localized to the endoplasmic reticulum (ER). It plays a key role in proper glycosylation, folding and assembly of newly synthesized membrane bound or secretory proteins. It also facilitates retention of mutant or defective proteins that are improperly folded and prevents translocation of such proteins from the cytosol to the ER lumen. The protein is induced under conditions of stress such as oxidative stress, chemical toxicity, glycosylation and hypoxia. It plays a crucial role in the maintenance of cell homeostasis and the prevention of apoptosis and acts as a biomarker of hypoglycemia. It has a neuroprotective function in neurons exposed to glutamate exotoxicity and oxidative stress.

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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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Customers Also Viewed

W W Li et al.
The Journal of biological chemistry, 268(16), 12003-12009 (1993-06-05)
The calcium ionophore A23187 has been shown to induce the expression of a set of glucose-regulated protein (GRP) genes through the depletion of Ca2+ from the intracellular Ca2+ stores. Here we demonstrate that thapsigargin, which inhibits specifically the endoplasmic reticulum
W W Li et al.
Molecular and cellular biology, 17(1), 54-60 (1997-01-01)
Previously, we have identified a constitutive nuclear factor, p70CORE, from HeLa cell nuclear extract which interacts specifically with the stress-inducible change region (SICR) of the grp78 promoter. Here we report that p70CORE is identical to YY1, a member of the
P L Mote et al.
Mechanisms of ageing and development, 104(2), 149-158 (1998-10-29)
The endoplasmic reticulum chaperone glucose-regulated protein 78 (GRP78) is essential for the proper glycosylation, folding and assembly of many membrane bound and secreted proteins. GRP78 mRNA is well known to be induced in cultured cells by lowering medium glucose concentrations
H Liu et al.
The Journal of biological chemistry, 272(35), 21751-21759 (1997-08-29)
Activation of stress response genes can impart cellular tolerance to environmental stress. Iodoacetamide (IDAM) is an alkylating toxicant that up-regulates expression of hsp70 (Liu, H., Lightfoot, D. L., and Stevens, J. L. (1996) J. Biol. Chem. 271, 4805-4812) and grp78
Z Yu et al.
Experimental neurology, 155(2), 302-314 (1999-03-11)
The 78-kDa glucose-regulated protein (GRP78) is localized in the endoplasmic reticulum (ER), and its expression is increased by environmental stressors in many types of nonneuronal cells. We report that levels of GRP78 are increased in cultured rat hippocampal neurons exposed

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The isolation of subcellular fractions by centrifugation is a commonly used technique and is widely applicable across multiple cell and tissue types. Because organelles differ in their size, shape, and density, centrifugation can be easily employed to separate and purify organelle fractions from gently homogenized samples.

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