This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 21.5 kDa. The protein migrates as 30-40 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
Human CD30 Ligand, His Tag, low endotoxin on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Immobilized Human CD30, Fc Tag (Cat. No. CD0-H5250) at 2 μg/mL (100 μL/well) can bind Human CD30 Ligand, His Tag, low endotoxin (Cat. No. CDL-H524b) with a linear range of 0.039-0.313 μg/mL (QC tested).
Loaded Biotinylated Human CD30, Avitag,His Tag (Cat. No. CD0-H82E6) on SA Biosensor, can bind Human CD30 Ligand, His Tag, low endotoxin (Cat. No. CDL-H524b) with an affinity constant of 132 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
FACS analysis shows that Human CD30 Ligand, His Tag, low endotoxin (Cat. No. CDL-H524b) can bind to K562-CD30 cells surface CD30. The concentration of Human CD30 Ligand is 3 μg/mL (Routinely tested).
FACS analysis shows that the binding of Human CD30 Ligand, His Tag, low endotoxin (Cat. No. CDL-H524b) to K562-CD30 cells surface CD30 was inhibited by increasing concentration of neutralizing anti-CD30 antibody. The concentration of Human CD30 Ligand used is 3 μg/mL. The IC50 is 0.2401 μg/mL (Routinely tested).
Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.
Price(USD) : $350.00
Price(USD) : $2310.00
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