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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human PITRM1, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 31.74 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Leu544-Ser806 |
Aliases /Synonyms | Pitrilysin metalloproteinase 1, hMP1, MP1, Metalloprotease 1, PREP, KIAA1104, Presequence protease, mitochondrial, PITRM1, hPreP |
Reference | ARO-P13307 |
Note | For research use only. |
Title: Introduction to Recombinant Human PITRM1
Recombinant Human PITRM1, also known as Presequence Protease, is a protein that plays a crucial role in the maintenance of mitochondrial function. It is a member of the M16 metallopeptidase family and is involved in the degradation of presequences of precursor proteins targeted to the mitochondria. In this article, we will explore the structure, activity, and application of Recombinant Human PITRM1.
Title: Structure of Recombinant Human PITRM1
Recombinant Human PITRM1 is a 100 kDa protein that contains 912 amino acids. It is composed of three domains: an N-terminal mitochondrial targeting sequence, a central catalytic domain, and a C-terminal domain. The catalytic domain is responsible for the proteolytic activity of PITRM1, while the C-terminal domain is involved in protein-protein interactions.
The catalytic domain of PITRM1 contains a highly conserved metallopeptidase motif, HEXXH, which is responsible for the hydrolysis of peptide bonds. This domain also contains a zinc-binding site, which is essential for the catalytic activity of PITRM1. The C-terminal domain of PITRM1 contains a coiled-coil motif, which is involved in the formation of homo-oligomers.
Title: Activity of Recombinant Human PITRM1
Recombinant Human PITRM1 is a highly specific protease that cleaves presequences of precursor proteins targeted to the mitochondria. It recognizes and cleaves peptides with a presequence motif of -[R/K]-[F/Y]-[L/I/V]-[K/R]-[H/Q]-[L/I/V]-[S/A]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-[L/I/V]-[L/I/V]-[A/G]-
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