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Merck

G4420

Sigma-Aldrich

Anti-GRP94 (C-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-Endoplasmin precursor, Anti-Glucose Regulated Protein 94, Anti-Tumor Rejection Antigen 1, Anti-gp96

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

formulario

buffered aqueous solution

mol peso

antigen 94 kDa

reactividad de especies

canine, human, mouse

concentración

~1 mg/mL

técnicas

immunocytochemistry: suitable
immunoprecipitation (IP): 10-20 μg using MDCK whole cell lysate
indirect immunofluorescence: 2-4 μg/mL using HeLa cells
microarray: suitable
western blot: 0.5-1 μg/mL using whole cell extracts of HeLa, MDCK, and NIH3T3 cells

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... HSP90B1(7184)
mouse ... Hsp90b1(22027)
rat ... Tra1(298957)

Categorías relacionadas

Inmunógeno

synthetic peptide corresponding to amino acids 733-750 located near the C-terminus of human GRP94. This sequence is identical in mouse, rat, dog, porcine, and bovine GRP94 and highly conserved (1 amino acid substitutuion) in chicken.

Aplicación

Anti-GRP94 (C-terminal) antibody produced in rabbit has been used in immunocytochemistry.
Anti-GRP94 (C-terminal) antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5-1μg/mL using whole cell extracts of the human epitheloid carcinoma HeLa cells, Madin Darby canine kidney (MDCK) cells, and mouse fibroblast NIH3T3 cells. It is also suitable for immunoprecipitation of GRP94 protein from a MDCK whole cell lysate at 10-20μg concentration.

Acciones bioquímicas o fisiológicas

GRP94 (glucose-regulated protein 94) is involved in protein folding, sorting and secretion, and binding of immunogenic peptides. GRP94 has a role in peptide antigen presentation to major histocompatibility complex class I molecules of antigen presenting cells (APCs). It binds specifically to CD91 (α2-macroglobulin receptor), and possibly to the Toll-like receptors (TLRs) on the surface of APCs. Overexpression of GRP94 has been associated with cellular transformation and tumorigenesis.
GRPs are unresponsive to heat stress and are induced by stress related to glucose starvation or defects in glycoprotein processing, depletion of Ca2+ stores, acidosis, and hypoxia conditions that are also common in poorly vascularized tumor tissues.
The GRP94 (glucose-regulated protein 94) is a 94 kDa Ca2+- binding glycoprotein that belongs to a subfamily of the heat shock proteins Hsp90. It is a chaperone protein constitutively localized to the endoplasmic reticulum (ER) of mammalian cells.

Forma física

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análisis (COA)

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Y Argon et al.
Seminars in cell & developmental biology, 10(5), 495-505 (1999-12-22)
GRP94 is the ER representative of the HSP90 family of stress-induced proteins. It binds to a limited number of proteins in the secretory pathway, apparently by recognizing advanced folding intermediates or incompletely assembled proteins, GRP94 also binds peptides and can
A Ménoret et al.
International journal of cancer, 56(3), 400-405 (1994-02-01)
Resistance to glucose starvation and expression of glucose-regulated proteins (grp) were studied in a model of rat colon carcinoma. In this model, various clones originating from the same parental tumor showed distinct tumorigenic potential in syngeneic hosts. Some clones were
Ramachandra K Reddy et al.
Cancer research, 62(24), 7207-7212 (2002-12-25)
A major challenge in treating cancer is the difficulty of bringing therapy to poorly perfused areas of solid tumors, which are often most resistant to chemotherapy and radiation. GRP94 is a chaperone protein localized in the endoplasmic reticulum with antiapoptotic
P K Srivastava et al.
Current opinion in immunology, 6(5), 728-732 (1994-10-01)
Heat shock proteins (HSPs) are associated with a broad spectrum of peptides derived from the cells from which they are isolated. Vaccination with such HSP-peptide complexes elicits protective immunity against tumors or other cells used as the source of HSPs.
A S Lee
Trends in biochemical sciences, 26(8), 504-510 (2001-08-16)
A protective mechanism used by cells to adapt to stress of the endoplasmic reticulum (ER) is the induction of members of the glucose-regulated protein (Grp) family. The induction of mammalian Grp proteins in response to ER stress involves a complex

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