E. coli Recombinant LON PROTEASE protein, His Tag (V2LY-0526-LY1774)

Name: E. coli Recombinant LON PROTEASE protein, His Tag
SKU: V2LY-0526-LY1774
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

E. coli

Protein Species

E. coli

Tag

His Tag

Protein Construction

This product is E. coli Recombinant LON PROTEASE protein, His Tag consist of Amino Acid: 1-784 and predicts a molecular mass of 88.3 kDa.

Molecule Mass

88.3 kDa

Sequence

Amino Acid: 1-784

Species

E. coli

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

Purity

>90% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile PBS

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

LONP1

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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