Protein Production
293FT, 293E, CHO

Truly Functional Protein
95% Purity
1-10 mg in 2 weeks

GeneExpressoMax™
293Expresso™

Transfection Reagents
* 90% Efficiency
* 95% Viability
* No sera interference
* Simple protocol
* High-throughput
* Only $98/ml

Baculovirus
Functional Protein
95% Purity
Fast turnaround
1-10 mg from Sf9 cells

Adenovirus, AAV
& Lentivirus

ORF or shRNA
* High Titer
* Cre, FLP, ΦC31
* Protein Kinases
* Transcription Factors
* Luciferases, GFP, RFP
* Protein Production
* Stable Cell Line


Excellgen

Jacqueline Lorayne Blankman
Scripps Research Institute

Project start date: 2008-12-01

Project end date: 2012-11-30


Sponsored Links Excellgen http://Excellgen.com

Recombinant Lentivirus & Adenovirus
High Yield and High Titer up to 1010 (lentivirus) and 1013 (adenovirus) for Guaranteed Expression of GOI. $3000, $2500
Baculovirus Protein Expression
Fast turn around, >95% purity functional protein. No outsourcing to China or India. $5500, $3950
Transient Protein Expression in CHO and HEK293 Cells
Transient Expression, Truly Functional Protein, 95% purity, 1~20 mg, fast turnaround. $5500, $3950

Jacqueline Lorayne Blankman
Scripps Research Institute

Project start date: 2008-12-01

Project end date: 2012-11-30



Grants awarded to Jacqueline Lorayne Blankman

Molecular Characterization Of Endocannabinoid Degradative Enzymes

Jacqueline Lorayne Blankman
Scripps Research Institute

Grant 1F31DA026261-01 from National Institute On Drug Abuse IRG: ZRG1

Abstract: The endocannabinoid system is the signaling network in the brain hijacked by the active component of marijuana, delta-9 tetrahydrocannibinol (THC), which elicits its effects primarily through activation of the central cannabinoid receptor (CB1) in the brain. The endocannabinoids 2-arachidonoylglycerol (2-AG) and anandamide (AEA) are the endogenous ligands of CB1 and are thought to modulate a diverse array of physiological processes including appetite, pain, emotions, cognition and addiction. Endocannabinoid levels in vivo are tightly regulated by enzymatic biosynthesis and degradation and, as such, these enzymes are principle regulators of EC signaling and tone. Degradation of AEA by the integral membrane protein fatty acid amide hydrolase (FAAH) has been well-characterized in vivo through the use of FAAH knockout mice and FAAH selective inhibitors. In contrast, the enzymes responsible for 2-AG termination have not been fully characterized. Using a functional proteomics approach, we identified three enzymes which collectively perform >98% of the 2-AG hydrolase activity in mouse brain proteomes monoacylglyceride lipase (MAGL), and the uncharacterized alpha/beta hydrolases 6 and 12 (ABHD6 and ABHD12). We propose to biochemically characterize the substrate selectivity, kinetic parameters and cellular/subcellular localization of recombinant preparations of MAGL, ABHD6 and ABHD12 and generate mouse models bearing targeted disruptions of these enzymes using genetic and pharmacological means. The results of these studies should allow the elucidation of the relative roles of these enzymes in endocannabinoid signaling and might also identify promising drug targets for therapeutics that elicit some of the medicinal benefits of THC without the psychoactive side-effects. The endocannabinoid 2-arachidonoylglycerol (2-AG) is a lipid neurotransmitter thought to mediate many (patho)physiological processes including obesity, pain, anxiety, depression and addiction. The goal of the proposed research is to elucidate the mechanisms by which 2-AG mediated signaling is terminated. The results of this study will increase the basic understanding of the endocannabinoid system and may also identify promising drug targets for the treatment of human diseases regulated by the endocannabinoid system

Project start date: 2008-12-01

Project end date: 2012-11-30