FAAH Protein (AA 1-579) (Strep Tag)

Catalog No. ABIN3131344

Product Details

Target: FAAH (Fatty Acid Amide Hydrolase (FAAH))

Protein Type: Recombinant

Protein Characteristics: AA 1-579

Origin: Mouse

Source: Cell-free protein synthesis (CFPS)

Purification tag / Conjugate: This FAAH protein is labelled with Strep Tag.

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Brand: AliCE®

Sequence: MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA GLETMDKAVQ RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH ASTLGLSLNE GVTSESDCVV VQVLKLQGAV PFVHTNVPQS MLSYDCSNPL FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK QSLEAAGHTL VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC LGDLVLVLKL PRWFKKLLSF LLKPLFPRLA AFLNSMCPRS AEKLWELQHE IEMYRQSVIA QWKAMNLDVV LTPMLGPALD LNTPGRATGA ISYTVLYNCL DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK KGIGLPVAVQ CVALPWQEEL CLRFMREVER LMTPEKRPS
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified in one-step affinity chromatography
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (AliCE®).

Purity: > 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Comment:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: FAAH (Fatty Acid Amide Hydrolase (FAAH))

Alternative Name: Faah (FAAH Products)

Background: Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Fatty acid ester hydrolase) (EC 3.1.1.-) (Oleamide hydrolase 1),FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:15533037, PubMed:32271712). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (PubMed:32271712). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (By similarity). {ECO:0000250|UniProtKB:P97612, ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712}.

Molecular Weight: 63.2 kDa

UniProt: O08914

Pathways: Monocarboxylic Acid Catabolic Process