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Rabbit Anti-LONP1 Recombinant Antibody (D8W1J) (CBMAB-P0472-YC)

Provided herein is a Rabbit monoclonal antibody against Human Lon peptidase 1, mitochondrial. The antibody can be used for immunoassay techniques, such as WB.
See all LONP1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
D8W1J
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Synthetic peptide corresponding to residues surrounding Gly887 of human PRSS15/LONP1
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid in 10 mM sodium HEPES, pH 7.5, 100ug/ml BSA, 150 mM sodium chloride, 0.02% sodium azide, 50% glycerol
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
LONP1
Introduction
LONP1 is a mitochondrial matrix protein that belongs to the Lon family of ATP-dependent proteases. This protein mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides in the mitochondrial matrix. It may also have a chaperone function in the assembly of inner membrane protein complexes, and participate in the regulation of mitochondrial gene expression and maintenance of the integrity of the mitochondrial genome.
Entrez Gene ID
Human9361
Mouse74142
Rat170916
UniProt ID
HumanP36776
MouseQ8CGK3
RatQ924S5
Alternative Names
PIM1; LON; PRSS15; hLON; LonHS; LONP; CODASS
Function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters (PubMed:12198491, PubMed:15870080, PubMed:17420247, PubMed:8248235).
Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, helicase Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575).
Biological Process
Cellular response to oxidative stressManual Assertion Based On ExperimentIDA:UniProtKB
Chaperone-mediated protein complex assemblyManual Assertion Based On ExperimentIBA:GO_Central
Mitochondrial DNA metabolic process1 PublicationNAS:UniProtKB
Mitochondrial genome maintenance1 PublicationNAS:UniProtKB
Mitochondrion organizationManual Assertion Based On ExperimentIMP:UniProtKB
Oxidation-dependent protein catabolic processManual Assertion Based On ExperimentIMP:UniProtKB
Protein quality control for misfolded or incompletely synthesized proteinsManual Assertion Based On ExperimentIBA:GO_Central
Proteolysis involved in cellular protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Response to hypoxiaManual Assertion Based On ExperimentIEP:UniProtKB
Cellular Location
Mitochondrion matrix
Involvement in disease
CODAS syndrome (CODASS):
A rare syndrome characterized by the combination of cerebral, ocular, dental, auricular, and skeletal features. These include developmental delay, craniofacial anomalies, cataracts, ptosis, median nasal groove, delayed tooth eruption, hearing loss, short stature, delayed epiphyseal ossification, metaphyseal hip dysplasia, and vertebral coronal clefts.

Xu, Z., Fu, T., Guo, Q., Zhou, D., Sun, W., Zhou, Z., ... & Gan, Z. (2022). Disuse-associated loss of the protease LONP1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength. Nature Communications, 13(1), 894.

Sheng, X., Liu, C., Yan, G., Li, G., Liu, J., Yang, Y., ... & Ding, L. (2022). The mitochondrial protease LONP1 maintains oocyte development and survival by suppressing nuclear translocation of AIFM1 in mammals. EBioMedicine, 75.

Zhao, K., Huang, X., Zhao, W., Lu, B., & Yang, Z. (2022). LONP1-mediated mitochondrial quality control safeguards metabolic shifts in heart development. Development, 149(6), dev200458.

Shin, C. S., Meng, S., Garbis, S. D., Moradian, A., Taylor, R. W., Sweredoski, M. J., ... & Chan, D. C. (2021). LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding. Nature Communications, 12(1), 265.

Maneix, L., Sweeney, M. A., Lee, S., Iakova, P., Moree, S. E., Sahin, E., ... & Catic, A. (2021). The mitochondrial protease LonP1 promotes proteasome inhibitor resistance in multiple myeloma. Cancers, 13(4), 843.

Pollecker, K., Sylvester, M., & Voos, W. (2021). Proteomic analysis demonstrates the role of the quality control protease LONP1 in mitochondrial protein aggregation. Journal of Biological Chemistry, 297(4).

Gibellini, L., De Gaetano, A., Mandrioli, M., Van Tongeren, E., Bortolotti, C. A., Cossarizza, A., & Pinti, M. (2020). The biology of Lonp1: More than a mitochondrial protease. International Review of Cell and Molecular Biology, 354, 1-61.

Besse, A., Brezavar, D., Hanson, J., Larson, A., & Bonnen, P. E. (2020). LONP1 de novo dominant mutation causes mitochondrial encephalopathy with loss of LONP1 chaperone activity and excessive LONP1 proteolytic activity. Mitochondrion, 51, 68-78.

Venkatesh, S., Li, M., Saito, T., Tong, M., Rashed, E., Mareedu, S., ... & Suzuki, C. K. (2019). Mitochondrial LonP1 protects cardiomyocytes from ischemia/reperfusion injury in vivo. Journal of molecular and cellular cardiology, 128, 38-50.

Ghosh, J. C., Seo, J. H., Agarwal, E., Wang, Y., Kossenkov, A. V., Tang, H. Y., ... & Altieri, D. C. (2019). Akt phosphorylation of mitochondrial Lonp1 protease enables oxidative metabolism and advanced tumor traits. Oncogene, 38(43), 6926-6939.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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