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Brand: ProteoGenix

Recombinant Human PITRM1, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
31.74 kDa

$392.00

100ug + 392 loyalty points
Leu544–Ser806
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Recombinant Human PITRM1, N-His

Recombinant Human PITRM1, N-His

Product name Recombinant Human PITRM1, N-His
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.
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 ProteoGenix
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.
Molecular Constructor
Leu544–Ser806

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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