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- Item 1 of 4Human LR3IGF1 protein [orb82618]Featured
ELISA, FA, HPLC, SDS-PAGE, WB
Unconjugated
> 95% pure by SDS-PAGE and HPLC analyses.
9.1 kDa
5 mg, 20 mg, 1 mg - Item 1 of 3Featured
The human full length CLDN18.2 Protein has a MW of 27.5 kDa
Mammalian
50 μg, 100 μg, 10 μg - Item 1 of 3Human GPRC5D full length protein-exo [orb1291764]Featured
The human full length GPRC5D Protein has a MW of 38.6 kDa
Mammalian
50 μg, 100 μg - Item 1 of 3Human CD24 full length protein-exo [orb1291768]Featured
The human CD24 Protein has a MW of 8.1 kDa
Mammalian
50 μg, 100 μg - Item 1 of 3Human TNFRSF11A Protein, hFc Tag [orb1291084]Featured
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 46.2 kDa after removal of the signal peptide. The apparent molecular mass of TNFRSF11A-hFc is approximately 55-70 kDa due to glycosylation.
Mammalian
100 μg, 10 μg, 50 μg - Item 1 of 3Human ITGB1 Protein, hFc Tag [orb1290974]Featured
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 104.5 kDa after removal of the signal peptide. The apparent molecular mass of ITGB1-hFc is approximately 130-250 kDa due to glycosylation.
Mammalian
10 μg, 50 μg, 100 μg - Item 1 of 3Human IL9R Protein, hFc Tag [orb1291063]Featured
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 60.83 kDa after removal of the signal peptide.
Mammalian
10 μg, 50 μg, 100 μg - Item 1 of 3Human IL15 Protein, hFc Tag [orb1291067]Featured
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 38.9 kDa after removal of the signal peptide. The apparent molecular mass of IL15-hFc is approximately 35-55kDa due to glycosylation.
Mammalian
50 μg, 10 μg, 100 μg 
- Item 1 of 4Sepharose Protein A [orb348753]
IP
Sepharose
Protein A has a high affinity for the Fc regions of IgG molecules from a variety of species, including human, mouse, rat IgG2c, cow IgG2c, goat IgG2, sheep IgG2, and rabbit. Immobilization of protein A creates an affinity resin that can be used to isolate IgG fractions from crude serum, ascites fluid or hybridoma supernatants/dilute cell cultures. High capacity and high flow rate fractionation is applicable to both laboratory and scale-up processes. Sepharose Protein A can be used for immunoprecipitation and purification of monoclonal antibodies.
2 ml
