G8918

Anti-GRP78/BiP (GL-19) antibody produced in rabbit

Name: Anti-GRP78/BiP (GL-19) antibody produced in rabbit
Brand: SIGMA

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

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

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About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

MDL number:

MFCD01865530

Product Name

Anti-GRP78/BiP (GL-19) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

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, hamster, human

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunocytochemistry: 1:1,000 using mouse fibroblasts NIH3T3 cells
microarray: suitable
western blot: 1:3,000 using human epitheloid carcinoma HeLa whole cell extract

UniProt accession no.

P11021

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Application

Anti-GRP78/BiP (GL-19) antibody produced in rabbit has been used in:

western blotting
immunocytochemistry
immunohistochemistry

Biochem/physiol Actions

GRP78 (78-kDa glucose-regulated protein) is essential for cell viability. GRP78/BiP is induced by stress-inducing agents or by conditions that adversely affect endoplasmic reticulum(ER) function, including oxidative stress, chemical toxicity, Ca²⁺ ionophores, inhibition of the ER Ca²⁺ -ATPase, inhibitors of glycosylation and hypoxia. GRP78/BiP is critical for maintenance of Ca²⁺homeostasis and the prevention of apoptosis. GRP78/BiP levels are reduced in Alzheimer′s disease brains and the decreased expression of GRP78/BiP is found associated with mis-sense mutations in presenilin-1 (PS-1).

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.

General description

GRP78/BiP is a Ca²⁺-binding molecular chaperone located in the endoplasmic reticulum (ER). It is a highly conserved protein.

Physical form

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

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Storage Class

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number

0000475637

0000440297

0000396602

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GRP78 at the centre of the stage in cancer and neuroprotection

Casas, Caty

Frontiers in Neuroscience, 11, 177-177 (2017)

miR-107 regulates granulin/progranulin with implications for traumatic brain injury and neurodegenerative disease

Wang WX, et al.

The American Journal of Pathology, 177(1), 334-345 (2010)

Differential light-induced responses in sectorial inherited retinal degeneration.

Eva Ramon et al.

The Journal of biological chemistry, 289(52), 35918-35928 (2014-11-02)

Retinitis pigmentosa (RP) is a group of genetically and clinically heterogeneous inherited degenerative retinopathies caused by abnormalities of photoreceptors or retinal pigment epithelium in the retina leading to progressive sight loss. Rhodopsin is the prototypical G-protein-coupled receptor located in the

Overexpressing GRP78 influences Ca2+ handling and function of mitochondria in astrocytes after ischemia-like stress

Ouyang YB, et al.

Mitochondrion, 11(2), 279-286 (2011)

Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.

Henning G Hansen et al.

Bioscience reports, 34(2) (2014-04-01)

In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1α and Ero1β. The activity of Ero1α is tightly regulated through the formation of intramolecular disulfide bonds to help

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