3-Oxoacyl-[acyl-carrier-protein] synthase 2 (fabF), Escherichia coli, recombinant

3-Oxoacyl-[acyl-carrier-protein] synthase 2 (fabF), Escherichia coli, recombinant
Item number Size Datasheet Manual SDS Delivery time Quantity Price
CSB-EP359466ENV.20 20 µg -

10 - 14 business days*

364.00€
CSB-EP359466ENV.100 100 µg -

10 - 14 business days*

667.00€
CSB-EP359466ENV.1 1 mg -

10 - 14 business days*

2,209.00€
 
Organism: Escherichia coli (strain K12). Source: E.coli. Expression Region: 2-413aa. Protein... more
Product information "3-Oxoacyl-[acyl-carrier-protein] synthase 2 (fabF), Escherichia coli, recombinant"
Organism: Escherichia coli (strain K12). Source: E.coli. Expression Region: 2-413aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: SKRRVVVTGL GMLSPVGNTV ESTWKALLAG QSGISLIDHF DTSAYATKFA GLVKDFNCED IISRKEQRKM DAFIQYGIVA GVQAMQDSGL EITEENATRI GAAIGSGIGG LGLIEENHTS LMNGGPRKIS PFFVPSTIVN MVAGHLTIMY GLRGPSISIA TACTSGVHNI GHAARIIAYG DADVMVAGGA EKASTPLGVG GFGAARALST RNDNPQAASR PWDKERDGFV LGDGAGMLVL EEYEHAKKRG AKIYAELVGF GMSSDAYHMT SPPENGAGAA LAMANALRDA GIEASQIGYV NAHGTSTPAG DKAEAQAVKT IFGEAASRVL VSSTKSMTGH LLGAAGAVES IYSILALRDQ AVPPTINLDN PDEGCDLDFV PHEARQVSGM EYTLCNSFGF GGTNGSLIFK KI. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. Reference: Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.Moche M., Schneider G., Edwards P., Dehesh K., Lindqvist Y.J. Biol. Chem. 274:6031-6034(1999). Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
Keywords: b1095, KAS II, Beta-ketoacyl-ACP synthase II, 3-oxoacyl-[acyl-carrier-protein] synthase 2, 3-oxoacyl-[acyl-carrier-protein] synthase II, Recombinant Escherichia coli 3-oxoacyl-[acyl-carrier-protein] synthase 2 (fabF)
Supplier: Cusabio
Supplier-Nr: EP359466ENV

Properties

Application: Activity not tested
Conjugate: No
Host: E.coli
Species reactivity: E.coli
MW: 58.9 kD
Purity: >90% (SDS-PAGE)

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
Information about the product reference will follow. more
You will get a certificate here
or to request a certificate of analysis.
Read, write and discuss reviews... more
Customer review for "3-Oxoacyl-[acyl-carrier-protein] synthase 2 (fabF), Escherichia coli, recombinant"
Write a review
or to review a product.
Viewed