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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

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 75 kDa

species reactivity

mouse, human, canine

concentration

~1 mg/mL

technique(s)

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Immunogen

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).

Application

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

Biochem/physiol Actions

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.

Target description

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

Physical form

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

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.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein
Wadhwa R, et al.
Experimental Cell Research, 274(2), 246-253 (2002)
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)
Molecular chaperones in cellular protein folding
Hartl EU, et al.
Nature, 381(6583), 571-571 (1996)
Organelle-associated rRNA Degradation
Parekh VS
The Journal of Biological Chemistry (2018)
Jinliang Huang et al.
Bio-protocol, 9(11), e3255-e3255 (2019-06-05)
Cytosolic rRNAs are highly dynamic and can be degraded under conditions such as apoptosis, starvation and magnesium depletion. The degradation is also related to their specific localization, as fractions of cytosolic ribosomes are localized on the surfaces of intracellular organelles

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