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AB125600

Recombinant Human Grp75/MOT protein

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Recombinant Human Grp75/MOT protein is a Human Full Length protein, in the 47 to 679 aa range, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE.

View Alternative Names

GRP75, HSPA9B, mt-HSP70, HSPA9, 75 kDa glucose-regulated protein, Heat shock 70 kDa protein 9, Heat shock protein family A member 9, Mortalin, Peptide-binding protein 74, GRP-75, MOT, PBP74

1 Images
SDS-PAGE - Recombinant Human Grp75/MOT protein (AB125600)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Grp75/MOT protein (AB125600)

SDS Page analysis of ab125600

Key facts

Purity

>80% Densitometry

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P38646

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

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SDS-PAGE - Recombinant Human Density Regulated Protein (His tag N-Terminus) (AB111640)

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Previously labelled as Grp75.
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Sequence info

[{"linker":null,"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"97 kDa","actualMolecularWeight":null,"aminoAcidEnd":679,"aminoAcidStart":47,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P38646","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Grp75 also known as MOT is a chaperone protein with a molecular mass of approximately 75 kDa. This protein is part of the heat shock protein 70 family and often referred to as Grp75 protein or MOT protein. Typically Grp75 is expressed in the mitochondria of eukaryotic cells. Its primary function lies in aiding the folding and assembly of newly synthesized proteins and responding to cellular stress conditions. The MOT-238 and MOT proteins are related variants in this protein family and antibodies like anti-MOT can specifically detect Grp75.
Biological function summary

Grp75 facilitates important cellular processes through its involvement in the regulation of mitochondrial homeostasis and cellular stress responses. Grp75 forms complexes with other mitochondrial proteins ensuring proper function of protein import and maintenance of mitochondrial DNA. It plays an essential role in the cellular response to stress by interacting with other heat shock proteins such as Hsp60 and by stabilizing proteins under conditions of thermal and oxidative stress. Additionally Grp75 is connected to the regulation of cell proliferation and apoptosis mechanisms integral to maintaining cellular balance.

Pathways

Grp75 is heavily involved in the mitochondrial unfolded protein response and apoptosis pathways. It associates with proteins like PINK1 and Parkin which are vital in the selective autophagy of mitochondria known as mitophagy. In response to misfolded proteins Grp75 helps to maintain mitochondrial function and promotes cell survival through interaction with other mitochondrial proteins. The JG1 and 9F8 proteins are also part of these pathways linked through their roles in protein quality control mechanisms within the cell.

Grp75 has been implicated in neurodegenerative diseases such as Parkinson's disease and certain cancers. Mutations or functional deficiencies in Grp75 can disrupt mitochondrial function which is a critical factor in the pathogenesis of Parkinson’s disease. The connection to proteins like PINK1 and Parkin in this context highlights the role Grp75 plays in the etiology of the disorder. In cancer Grp75 contributes to the cellular stress response and its overexpression can lead to drug resistance making it a target of interest for developing therapeutic strategies.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

Function

Mitochondrial chaperone that plays a key role in mitochondrial protein import, folding, and assembly. Plays an essential role in the protein quality control system, the correct folding of proteins, the re-folding of misfolded proteins, and the targeting of proteins for subsequent degradation. These processes are achieved through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones (PubMed : 18632665, PubMed : 25615450, PubMed : 28848044, PubMed : 30933555, PubMed : 31177526). In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins (By similarity). Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis, interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed : 26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed : 21123823, PubMed : 26702583). Regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, providing calcium for the downstream calcium channel MCU, which releases it into the mitochondrial matrix (By similarity). Although primarily located in the mitochondria, it is also found in other cellular compartments. In the cytosol, it associates with proteins involved in signaling, apoptosis, or senescence. It may play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (PubMed : 24625977, PubMed : 26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). Protects against reactive oxygen species (ROS) (By similarity). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (PubMed : 16091382).

Sequence similarities

Belongs to the heat shock protein 70 family.

Subcellular localisation

Mitochondrion

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Product protocols

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Target data

Mitochondrial chaperone that plays a key role in mitochondrial protein import, folding, and assembly. Plays an essential role in the protein quality control system, the correct folding of proteins, the re-folding of misfolded proteins, and the targeting of proteins for subsequent degradation. These processes are achieved through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones (PubMed : 18632665, PubMed : 25615450, PubMed : 28848044, PubMed : 30933555, PubMed : 31177526). In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins (By similarity). Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis, interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed : 26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed : 21123823, PubMed : 26702583). Regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, providing calcium for the downstream calcium channel MCU, which releases it into the mitochondrial matrix (By similarity). Although primarily located in the mitochondria, it is also found in other cellular compartments. In the cytosol, it associates with proteins involved in signaling, apoptosis, or senescence. It may play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (PubMed : 24625977, PubMed : 26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). Protects against reactive oxygen species (ROS) (By similarity). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (PubMed : 16091382).
See full target information HSPA9
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