PBS pH7.5, DTT 1mM, 0.5mM Zwittergent 3-14 and 10% Glycerol if refolding. PBS, Urea 8M if denaturing conditions
Form
liquid
Delivery condition
Dry Ice
Delivery lead time in business days
Europe: 5-7 working days
USA & Canada: 7-10 working days
Rest of the world: 5-12 working days
Storage condition
Lipase protein is stored:
At 4°C for short term period (less than a week)
At -20°C or -80°C for long term period
Recommendations
It is important to avoid avoid freezing/thawing cycles
20-40% glycerol may be added to improve cryoprotection
Brand
ProteoGenix
Host species
Escherichia coli (E.coli)
Fragment Type
Partial
Protein Accession
YP_056770.1
Spec:Entrez GeneID
2932970
Spec:SwissProtID
Q6A601
NCBI Reference
YP_056770.1
Aliases /Synonyms
LIPASE, triacylglycerol lipase precursor
Reference
PX-P1121
Note
For research use only
Description of Lipase Protein/ Propionibacterium Acnes LIPASE Recombinant Protein
Introduction:
Propionibacterium acnes is a Gram-positive bacterium that is commonly found on human skin. While it is a normal resident of the skin microbiome, it is also known to be a major contributor to acne vulgaris, a common skin condition that affects millions of people worldwide. One of the key enzymes produced by this bacterium is the lipase protein, which has been identified as a potential drug target for the treatment of acne. In this article, we will delve into the structure, activity, and potential applications of the Propionibacterium acnes lipase protein, also known as LIPASE Recombinant Protein.
Structure of LIPASE Recombinant Protein:
The LIPASE Recombinant Protein is a 33 kDa enzyme that belongs to the serine hydrolase family. It is composed of 299 amino acids and has a conserved catalytic triad of Ser-Asp-His, which is essential for its enzymatic activity. The crystal structure of this protein has been determined, revealing a classical α/β hydrolase fold with a central seven-stranded β-sheet surrounded by eight α-helices. The active site of the enzyme is located at the interface of these two secondary structures, with the catalytic triad residues positioned in a pocket that is accessible to the substrate.
Activity of LIPASE Recombinant Protein:
Lipase enzymes are known for their ability to hydrolyze ester bonds, making them essential for the breakdown of lipids. The LIPASE Recombinant Protein from Propionibacterium acnes is no exception, as it has been shown to exhibit high lipolytic activity. In fact, studies have demonstrated that this enzyme is able to efficiently hydrolyze a wide range of triglycerides, including those found in human sebum, the oily substance that contributes to the development of acne. This lipolytic activity is crucial for the survival and virulence of Propionibacterium acnes, as it allows the bacterium to utilize lipids as a source of energy and to modulate the composition of the skin’s lipid barrier.
Potential Applications of LIPASE Recombinant Protein:
Given the role of LIPASE Recombinant Protein in the pathogenesis of acne, it has been identified as a potential drug target for the treatment of this common skin condition. One approach is to develop inhibitors that can block the activity of this enzyme, thereby reducing the production of inflammatory lipids and preventing the formation of acne lesions. Another potential application is the use of this enzyme as a diagnostic tool, as its presence and activity can serve as a marker for the presence of Propionibacterium acnes on the skin.
Conclusion:
In summary, the lipase protein from Propionibacterium acnes, also known as LIPASE Recombinant Protein, is a key enzyme involved in the development of acne. Its crystal structure has been determined, revealing a classical α/β hydrolase fold with a conserved catalytic triad. This enzyme exhibits high lipolytic activity, which is crucial for the survival and virulence of Propionibacterium acnes. Its potential as a drug target and diagnostic tool makes it an important focus of research for the treatment and management of acne.
Reviews
There are no reviews yet.