Analytical Data
-
Gene name
LCAT
- Application
-
Alternative Names
LCAT;Phosphatidylcholine-sterol acyltransferase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P04180
-
Expression Region
25-440aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E
-
Molecular Weight
50 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
LCAT (Lecithin-Cholesterol Acyltransferase) is a pivotal enzyme in lipid metabolism, primarily involved in the esterification of cholesterol in the bloodstream. It plays a crucial role in the proper functioning of high-density lipoproteins (HDL), which are essential for reverse cholesterol transport, a process that removes excess cholesterol from peripheral tissues and transports it to the liver for excretion. Dysregulation of LCAT can lead to lipid disorders and is associated with various cardiovascular diseases. In the context of biomedical research, the recombinant production of LCAT has emerged as a significant area of interest, as it allows for the detailed study of enzyme mechanisms, structure-function relationships, and the potential development of therapeutic applications. Researchers aim to produce LCAT in heterologous systems, such as bacteria or yeast, to obtain sufficient quantities of pure enzyme for biochemical assays, structural analysis, and rational drug design. Additionally, understanding the molecular dynamics of LCAT can provide insights into its role in HDL metabolism and its implications for diseases like atherosclerosis. Overall, the study of recombinant LCAT presents a valuable opportunity for advancing our knowledge of lipid metabolism and improving strategies for managing lipid-related health issues.
