Neurotransmitter Receptors, Transporters, and Ion Channels
S100A9
Product Name
S100A9 Protein, Human, Recombinant (His Tag)
Synonyms
60B8AG Protein, Human; CAGB Protein, Human; CFAG Protein, Human; CGLB Protein, Human; L1AG Protein, Human; LIAG Protein, Human; MAC387 Protein, Human; MIF Protein, Human; MRP-14 Protein, Human; MRP14 Protein, Human; NIF Protein, Human; P14 Protein, Human
Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured by its binding ability in a functional ELISA. Immobilized S100A8-His at 10 μg/ml (100 μl/well) can bind S100A9-His (Cat: 11145-H08B), The EC50 of S100A9-His (Cat: 11145-H08B) is 0.35-0.70 μg/mL.
Protein Construction
A DNA sequence encoding the human S100A9 (NP_002956.1) (Met 1-Pro 114) was expressed, fused with a polyhistidine tag at the C-terminus.
Expressed Host
Baculovirus-Insect Cells
Molecule Mass
The recombinant human S100A9 consists of 124 amino acids and predicts a molecular mass of 14.6 kDa. It migrates as an approximately 16 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile PBS, pH 7.4Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.