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Merck

G4045

Sigma-Aldrich

Anti-GRP75 (SQ-15) antibody produced in rabbit

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

Sinónimos:

Anti-Glucose Regulated Protein 75, Anti-Mitochondrial Hsp70, Anti-Mortalin, Anti-Peptide Binding Protein 74

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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 75 kDa

reactividad de especies

mouse, human, canine

concentración

~1 mg/mL

técnicas

indirect immunofluorescence: 1-2 μg/mL using HeLa cells
western blot: 0.2-0.4 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

mouse ... Hspa9(15526)
rat ... Hspa9(291671)

Descripción general

GRP75 (glucose-regulated protein 75) belongs to a Hsp70 family of the heat shock proteins.
GRPs are unresponsive to heat stress and are induced by stress related to glucose starvation or defects in glycoprotein processing. GRP75/mortalin has been localized mainly to the endoplasmic reticulum (ER), but also to various cellular compartments including mitochondria and cytoplasmic vesicles.

Inmunógeno

synthetic peptide corresponding to amino acids 665-679 located at the C-terminus of human GRP75. This sequence is identical in mouse GRP75 (mot-1 and mot-2 isoforms) and highly conserved in rat (1 amino acid substitution).

Aplicación

Anti-GRP75 antibody produced in rabbit has been used in :
  • immunofluorescence
  • immunoblotting
  • immunocytochemistry

Acciones bioquímicas o fisiológicas

GRP75 (glucose-regulated protein 75) is involved in stress responses to intracellular trafficking, antigen processing, and control of cell proliferation, differentiation, and tumorigenesis. It is induced by low levels of ionizing radiation, glucose deprivation, calcium ionophore, and ozone and its levels correlate with muscle activity, mitochondrial activity, and biogenesis.
Heat shock proteins (HSP) are considered to function as molecular chaperones by transiently binding to newly synthesized proteins to facilitate their correct folding and assembly. GRP75 levels are associated with muscle activity, mitochondrial function and biogenesis.

Descripción de destino

GRP75 (SQ-15) encodes a heat-shock cognate protein. This protein plays a role in the control of cell proliferation.

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)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Travis J Cook et al.
Brain pathology (Zurich, Switzerland), 26(1), 75-81 (2015-06-23)
Mortalin, an essential mitochondrial chaperone protein, has previously been implicated in the pathogenesis of a wide array of diseases, including neurodegenerative conditions such as Parkinson's disease (PD) and Alzheimer's disease. Previous reports have consistently described mortalin protein levels to be
Organelle-associated rRNA Degradation
Parekh VS
The Journal of Biological Chemistry (2018)
Molecular chaperones in cellular protein folding
Hartl EU, et al.
Nature, 381(6583), 571-571 (1996)
Organelle-associated rRNA Degradation
Parekh VS
Test (2018)
Mortalin is expressed by astrocytes and decreased in the midbrain of Parkinson's disease patients
Cook TJ, et al.
Brain Pathology, 26(1), 75-81 (2016)

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