Seed linoleate 13S-lipoxygenase-1 (LOX1.1), Recombinant Protein
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Seed linoleate 13S-lipoxygenase-1 (LOX1.1), Recombinant Protein

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Cat: RP18682
Size: 0.5 mg (E-Coli)/ 0.05 mg (Baculovirus)/ 0.5 mg (Yeast)/ 0.05 mg (Mammalian-Cell)/ 1 mg (E-Coli)/ 0.1 mg (Baculovirus)/ 0.5 mg (Baculovirus)/ 1 mg (Yeast)/ 0.1 mg (Mammalian-Cell)/ 1 mg (Baculovirus)
Species: Glycine max (Soybean) (Glycine hispida)
Datasheet:

Product Info

Full Product Name
Recombinant Glycine max Seed linoleate 13S-lipoxygenase-1 (LOX1.1), partial
Product Gene Name
LOX1.1 recombinant protein
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Sequence
PKNELEVNPD GSAVDNLNAF LGRSVSLQLI SATKADAHGK GKVGKDTFLE GINTSLPTLG AGESAFNIHF EWDGSMGIPG AFYIKNYMQV EFFLKSLTLE AISNQGTIRF VCNSWVYNTK LYKSVRIFFA
Sequence Positions
16-145, Partial, provide the PLAT domain.
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
94,369 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.
Protein Family
Seed linoleate 13S-lipoxygenase

NCBI/Uniprot Data

NCBI Accession #
NP_001236153.1
NCBI GI #
351727907
NCBI GenBank Nucleotide #
NM_001249224.1
NCBI GeneID
547923
NCBI Official Full Name
seed linoleate 13S-lipoxygenase-1
NCBI Official Symbol
LOX1.1  
NCBI Official Synonym Symbols
L-1; Lx1  
NCBI Protein Information
seed linoleate 13S-lipoxygenase-1
UniProt Gene Name
LOX1.1  
UniProt Synonym Gene Names
LOX1; L-1  
UniProt Protein Name
Seed linoleate 13S-lipoxygenase-1
UniProt Synonym Protein Names
Lipoxygenase-1; L-1
UniProt Primary Accession #
P08170
UniProt Related Accession #
P08170
UniProt Comments
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.

For research use only, not for clinical use.