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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

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A Tomida et al.
International journal of cancer, 68(3), 391-396 (1996-11-04)
The glucose-regulated stress response in mammalian cells is characterized by the increased synthesis of glucose-regulated proteins (GRPs). In this study, we found that GRP-inducing conditions in culture led to induction of resistance to the topoisomerase I-targeted drug camptothecin in human
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
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
S L Sanders et al.
Cell, 69(2), 353-365 (1992-04-17)
Secretory proteins are segregated from cytosolic proteins by their translocation into the endoplasmic reticulum (ER). A modified secretory protein trapped during translocation across the ER membrane can be crosslinked to two previously identified proteins, Sec61p and BiP (Kar2p). The dependence
Z Muresan et al.
Molecular endocrinology (Baltimore, Md.), 12(3), 458-467 (1998-03-26)
To examine how binding of BiP (a molecular chaperone of the hsp70 family that resides in the endoplasmic reticulum) influences the conformational maturation of thyroglobulin (Tg, the precursor for thyroid hormone synthesis), we have developed a system of recombinant Tg

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