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α1-proteinase inhibitor In Vitro Transcribed mRNA-LNP
SG-MRNA-LNP-1873
α1-proteinase inhibitor In Vitro Transcribed mRNA-LNP
Source:The ORF of α1-proteinase inhibitorwas cloned in our IVT vector and mRNA was prepared through in vitro transcription and purification. The purified mRNA was further encapsulated with LNP(DSPC:Cholesterol:DMG-PEG:SM102).
Alternative Names:α1-proteinase inhibitor
SKU:SG-MRNA-LNP-1873-DCPS
Product Name:α1-proteinase inhibitor In Vitro Transcribed mRNA-LNP(DSPC:Cholesterol:DMG-PEG:SM102)
Product Description:α1-proteinase inhibitor In Vitro Transcribed mRNA encapsulated with LNP(DSPC:Cholesterol:DMG-PEG:SM102)
SKU:SG-MRNA-LNP-1873-DCPS
Product Name:α1-proteinase inhibitor In Vitro Transcribed mRNA-LNP(DSPC:Cholesterol:DMG-PEG:SM102)
Product Description:α1-proteinase inhibitor In Vitro Transcribed mRNA encapsulated with LNP(DSPC:Cholesterol:DMG-PEG:SM102)
PROPERTIES
Cap:
m7GpppN
5'-UTR:
5' -untranslated region derived from human alpha-globin RNA with an optimized Kozak sequence
ORF:
α1-proteinase inhibitor
3'-UTR:
3' UTR comprising two sequence elements derived from the aminoterminal enhancer of split (AES) mRNA and the mitochondrial encoded 12S ribosomal RNA
Poly(A) Tail:
A 110-nucleotide poly(A)-tail consisting of a stretch of 30 adenosine residues, followed by a 10-nucleotide linker sequence and another 70 adenosine residues.
Modifications:
N1-methyl-pseudouridine
Neutral Lipid:
1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC)
Cholesterol:
Cholesterol
Lonizable Lipid:
1,2-dimyristoyl-rac-glycero-3-methoxypolyethylene glycol-2000 (PEG2000-DMG)
PEG-lipid:
Heptadecan-9-yl 8-((2-hydroxyethyl)(8-(nonyloxy)− 8-oxooctyl)amino)octanoate)(SM-102)
Storage:
-20 °C
Buffer:
PBS, pH7.4
Cryoprotectant:
Trehalose
Background

Gene Alias

α1-proteinase inhibitor

Background

Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

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