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Merck
모든 사진(5)

Key Documents

G9043

Sigma-Aldrich

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

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

동의어(들):

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

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About This Item

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

생물학적 소스

rabbit

결합

unconjugated

항체 형태

IgG fraction of antiserum

항체 생산 유형

primary antibodies

클론

polyclonal

형태

buffered aqueous solution

분자량

antigen 78 kDa

종 반응성

mouse, chicken, Xenopus, hamster, human, rat

향상된 검증

independent
Learn more about Antibody Enhanced Validation

기술

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 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

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

애플리케이션

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.

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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


시험 성적서(COA)

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문서 라이브러리 방문

The unfolded protein response is activated in Alzheimer?s disease
Hoozemans J J M, et al.
Acta Neuropathologica, 110(2), 165-172 (2005)
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
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
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
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

문서

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

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