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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

Synonyme(s) :

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

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 78 kDa

Espèces réactives

mouse, chicken, Xenopus, hamster, human, rat

Validation améliorée

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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.
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
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
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

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Centrifugation separates organelles based on size, shape, and density, facilitating subcellular fractionation across various samples.

Centrifugation separates organelles based on size, shape, and density, facilitating subcellular fractionation across various samples.

Centrifugation separates organelles based on size, shape, and density, facilitating subcellular fractionation across various samples.

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