Recombinant Human Grp75/MOT protein is a Human Full Length protein, expressed in Escherichia coli, with >=80% purity and suitable for SDS-PAGE, WB.
>=80% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, WB
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Chaperone protein which 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). 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). Molecular adapter that 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, thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
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
Recombinant Human Grp75/MOT protein is a Human Full Length protein, expressed in Escherichia coli, with >=80% purity and suitable for SDS-PAGE, WB.
>=80% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, WB
No
No
Human
Constituents: 3% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl
Full Length
75 kDa
Recombinant
His tag N-Terminus
Liquid
ab115711 is purified by multi-step chromatography
Chaperone protein which 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). 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). Molecular adapter that 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, thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
Belongs to the heat shock protein 70 family.
Mitochondrion, Nucleus, Nucleolus
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Previously labelled as Grp75.
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.
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.
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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SDS-PAGE analysis:
Lane 1: MW marker
Lane 2: ab115711 at 1 μg
Lane 3: ab115711 at 2 μg
Lane 4: ab115711 at 5 μg
All lanes: Grp75 / MOT antibody
Lane 1: Western blot - Recombinant Human Grp75/MOT protein (ab115711) at 0.1 µg
Lane 2: HeLa cell lysate (heat shocked)
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