Anti-Mortalin/GRP75 Antibody (N52A/42)
Our mouse Mortalin/GRP75 monoclonal antibody from NeuroMab is produced in-house from clone N52A/42. It detects C. elegans, human, mouse, non-human primate, and rat Mortalin/GRP75 and is purified by Protein A chromatography. Works in WB, IHC, ICC, IP, ELISA.
C. elegans, Human, Mouse, Non-Human Primate, Rat
ELISA, ICC, IHC, IP, WB
Mouse
SKU: 75-127
Ships: 1-2 business days
Product Details
Mortalin/GRP75
Mitochondrial stress-70 protein or Mortalin/GRP75 is encoded by the gene HSPA9. Mortalin is a chaperone protein and plays a role in cell proliferation, stress response and mitochondria maintenance. It is widely expressed in tissues in mitochondria, endoplasmic reticulum, plasma membrane and cytoplasmic vesicles. Diseases associated with this gene include Even-Plus Syndrome and Sideroblastic Anemia 4.
Purified by Protein A chromatography
1 mg/mL
Monoclonal
N52A/42
IgG1
ELISA, ICC, IHC, IP, WB
Mouse
Hspa9 Grp75 Hsp74 Hspa9a
75 kDa
Identified as off-target mAb in screen for anti-Salm2 NeuroMabs (immunogen was fusion protein amino acids 551-766 of mouse SALM2). Target identified as Mortalin/Grp75 by LC-MS/MS analysis of protein immunopurified from rat brain using N52A/42.
Mouse
C. elegans, Human, Mouse, Non-Human Primate, Rat
AB_2120479
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.54
WB: 1:1000
ICC: 1:200
ICC: 1:200
Unconjugated
No cross-reactivity reported
Each new lot of antibody is quality control tested by western blot on rat whole brain lysate and confirmed to stain the expected molecular weight band.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
24 months from date of receipt
74kDa; Stress-70 protein; Grp75; 75 kDa glucose-regulated protein; Hsc74; GRP-75; Hsp74; Heat shock 70 kDa protein 9; Hsp74a; Mortalin; Hspa9a; Peptide-binding protein 74; PBP74; Mot-2; p66 MOT; Mot2; Mthsp70; mitochondrial; C3H-specific antigen; heat shock protein 9A; heat shock protein cognate 74; heat shock protein; 74 kDa
P38647
UniProt Summary: 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. In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins. Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. 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. 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. May play a role in the control of cell proliferation and cellular aging. Protects against reactive oxygen species (ROS). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex.
UniProt Summary: 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. In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins. Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. 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. 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. May play a role in the control of cell proliferation and cellular aging. Protects against reactive oxygen species (ROS). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex.
15526
Shipped on ice packs

