Lon protease homolog, mitochondrial (LONP1),partial, human, recombinant

Lon protease homolog, mitochondrial (LONP1),partial, human, recombinant
Item number Size Datasheet Manual SDS Delivery time Quantity Price
CSB-EP013032HU.20 20 µg -

10 - 14 business days*

292.00€
CSB-EP013032HU.100 100 µg -

10 - 14 business days*

533.00€
CSB-EP013032HU.1 1 mg -

10 - 14 business days*

2,209.00€
 
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 124-368aa. Protein Length:... more
Product information "Lon protease homolog, mitochondrial (LONP1),partial, human, recombinant"
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 124-368aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: LPLIAITRNP VFPRFIKIIE VKNKKLVELL RRKVRLAQPY VGVFLKRDDS NESDVVESLD EIYHTGTFAQ IHEMQDLGDK LRMIVMGHRR VHISRQLEVE PEEPEAENKH KPRRKSKRGK KEAEDELSAR HPAELAMEPT PELPAEVLMV EVENVVHEDF QVTEEVKALT AEIVKTIRDI IALNPLYRES VLQMMQAGQR VVDNPIYLSD MGAALTGAES HELQDVLEET NIPKRLYKAL SLLKK. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 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. Relevance: 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. Reference: "The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes." Kunova N., Ondrovicova G., Bauer J.A., Bellova J., Ambro L., Martinakova L., Kotrasova V., Kutejova E., Pevala V. Sci. Rep. 7:631-631(2017). Function: nan
Keywords: LONP, LONHs, PRSS15, Serine protease 15, Lon protease-like protein, Lon protease homolog, mitochondrial, Mitochondrial ATP-dependent protease Lon, Recombinant Human Lon protease homolog, mitochondrial (LONP1),partial
Supplier: Cusabio
Supplier-Nr: EP013032HU

Properties

Application: Activity not tested
Conjugate: No
Host: E.coli
Species reactivity: human
MW: 35.6 kD
Purity: >90% (SDS-PAGE)

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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