Recombinant Human Lon Protease Homolog, Mitochondrial (LONP1) Protein (His&Myc)

Name: Recombinant Human Lon Protease Homolog, Mitochondrial (LONP1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07037P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Lon Protease Homolog, Mitochondrial (LONP1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P36776
Target Symbol	LONP1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	LPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKK
Expression Range	124-368aa
Protein Length	Partial
Mol. Weight	35.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. 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.
Subcellular Location	Mitochondrion matrix.
Protein Families	Peptidase S16 family
Database References	HGNC: 9479 OMIM: 600373 KEGG: hsa:9361 STRING: 9606.ENSP00000353826 UniGene: Hs.350265
Associated Diseases	CODAS syndrome (CODASS)
Tissue Specificity	Duodenum, heart, lung and liver, but not thymus.

Gene Functions References

mitochondrial ATP-dependent Lon protease may serve as a potential biomarker for cancer diagnosis and novel target for the development of anticancer drugs and for predicting of the efficiency and effectiveness of chemotherapy of a variety of cancers. PMID: 29178076
We demonstrate that Lon plays a key role in glioma cell hypoxic survival and mitochondrial respiration, and propose Lon as a promising therapeutic target in the treatment of malignant gliomas. PMID: 27764809
Some features were not consistent with CODAS syndrome but overlapped with Marinesco-Sjogren syndrome, a multisystem disorder caused by a mutation in SIL1. An atypical mutation site may result in atypical presentation of the LONP1 mutation PMID: 28148925
LONP1 function and implication in human aging and disease was reviewed. PMID: 27387767
we observed that Lon protease downregulation is linked to a higher lipofuscinogenesis whereas the application of the mitochondrial-targeted antioxidant mitoTEMPO is able to prevent the accumulation of this protein aggregate. PMID: 28160744
Lon preferentially degrades the phosphorylated subunits of CcO and plays a role in the regulation of CcO activity in hypoxia and ischemia/reperfusion injury. PMID: 28442264
Lon protease (Lonp1), which is a key inductive of mitochondrial unfolded protein response (UPR(mt)) and is required to maintain the mitochondrial quality, was greatly induced in H. pylori infected gastric epithelial cells. PMID: 27108387
This analysis revealed that LONM specifically recognises and degrades unfolded, but not aggregated proteins. PMID: 26627475
Mutations of Lon, which likely impair its chaperone properties, are at the basis of a genetic inherited disease named the cerebral, ocular, dental, auricular, skeletal (CODAS) syndrome. (Review) PMID: 27033304
Inhibition of Lon protease by triterpenoids alters mitochondria and is associated to cell death in human cancer cells. PMID: 26314956
Lon downregulation attenuated hypoxia-induced cardiomyocyte apoptosis through a reduction of reactive oxygen species level. PMID: 25922169
LONP1 encodes an enzyme of bacterial ancestry that participates in protein turnover within the mitochondrial matrix, and mutations in its ATP-binding and proteolytic domains cause CODAS syndrome. PMID: 25808063
A review on the recent discoveries concerning Lon Protease functions. [review] PMID: 26363553
These results suggest that the mechanism underlying cell survival regulated by Lon is mediated by the maintenance of the protein stability of Hsp60-mtHsp70 complex. PMID: 25675302
Silencing of SIRT3 increased the levels of Lon protein and of its acetylation, suggesting that Lon is a target of SIRT3, likely at K917. PMID: 25128872
the structure of human mitochondrial Lon (hLon) protease, is reported. PMID: 25369343
We establish a link between LONP1 and CODAS syndrome in humans. PMID: 25574826
Lonp1 has a protective role against ochratoxin a induced cytotoxicity in kidney cells. PMID: 24565693
StAR proteolysis is executed by at least 2 mitochondrial proteases, the matrix LON protease and the inner membrane complexes of the metalloproteases AFG3L2 and AFG3L2:SPG7/paraplegin. PMID: 24422629
Lon protease deficiency led to an increase in ROS production and to an accumulation of carbonylated protein in the mitochondria. PMID: 24355201
Down-regulation of overexpressed human LON in cervical cancer suppresses cell proliferation and bioenergetics. PMID: 24260536
Data indicate that SDH5 is protected from mitochondrial LON protease (LONM)-mediated degradation in mitochondria by its stable interaction with SDHA, a state that is dysregulated in hereditary paraganglioma 2 (PGL2). PMID: 24414418
Lon is overexpressed specifically in various types of cancer tissue including oral cancer. PMID: 23788038
In cells with normal mitochondrial DNA levels, phosphorylated TFAM is degraded by Lon. PMID: 23201127
Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells. PMID: 21659532
Downregulation of mitochondrial lon protease impairs mitochondrial function and causes hepatic insulin resistance in human liver SK-HEP-1 cells. PMID: 21347624
The promoter of Lon is at least part responsible for the upregulation of this protein during oxidative stress. PMID: 20933102
Data show that Lon gene can be significantly downregulated by introduction of siRNA to result in enhanced sensitivity of MCF7 cells to UV, cisplatin and heat stress. PMID: 17584658
may prevent extensive oxidation, aggregation and accumulation of aconitase, which could otherwise compromise mitochondrial function and cellular viability PMID: 12198491
Lon participates directly in the metabolism of mtDNA. PMID: 14739292
results indicate that mitochondrial Lon is required for normal survival and proliferation; a clear impetus for Lon's evolutionary conservation PMID: 15683722
Results demonstrate that mitochondrial DNA binding is a physiological function of Lon and that cellular levels of Lon influence sensitivity to mtDNA damage. PMID: 17420247
A review of the current knowledge on both catalytic mechanisms and inhibitors of Lon protease. PMID: 18021745
Electrophoretic mobility shift assay and circular dichroism show that ssDNAs with a propensity for forming parallel G-quartets are specifically bound by hLon. PMID: 18174225

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.