Purity
Greater than 90% as determined by SDS-PAGE.
Alternative Names
(2E; 6E)-farnesyl diphosphate synthase; Dimethylallyltranstransferase; Farnesyl diphosphate synthase; Farnesyltranstransferase; Geranylgeranyl diphosphate synthase 1; Geranylgeranyl diphosphate synthase; Geranylgeranyl pyrophosphate synthase; Geranylgeranyl pyrophosphate synthetase; Geranyltranstransferase; GGPP synthase; GGPP synthetase; GGPPS; GGPPS_HUMAN; GGPPS1; GGPPSase; GGPS1; OTTHUMP00000036073; OTTHUMP00000216161; OTTHUMP00000216163; OTTHUMP00000216164
Species
Homo sapiens (Human)
Expression Region
1-300aa
Target Protein Sequence
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Protein Length
Full Length
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the
glycerol content, please remark when you place the order.
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 Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
This Human GGPS1 recombinant protein was produced in E.coli, where the gene sequence encoding Human GGPS1 (1-300aa) was expressed with the N-terminal 6xHis-SUMO tag. The purity of this GGPS1 protein was greater than 90% by SDS-PAGE.
Geranylgeranyl pyrophosphate synthase (GGPS1) is a key enzyme in plant terpenoid biosynthesis. The enzyme catalyzes the synthesis of geranylgeranyl pyrophosphate (GGPP), which is a precursor to several holoterpenoids (carotenoids, kaurene, diterpenes) and meroterpenoids (side-chain of chlorophylls, tocopherols, plastoquinones, phylloquinones). The study identified a cDNA for the plastid-located GGPS1 from Capsicum annuum and showed a correlative increase in enzyme activity and transcript level during fruit ripening. The cloned cDNA codes for a high molecular weight precursor of 369 amino acids which contains a transit peptide of approximately 60 amino acids. In-situ immunolocalization experiments have demonstrated that geranylgeranyl pyrophosphate synthase is located exclusively in the plastids.
Reference:
Kuntz M, Römer S, Suire C, Hugueney P, Weil JH, Schantz R, Camara B. Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening. Plant J. 1992 Jan;2(1):25-34.
