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Catalog Number | orb1494817 |
---|---|
Category | Proteins |
Description | Interleukin-5 (IL-5), produced by mast cells, T cells and eosinophils, is responsible for the activities attributed to eosinophil differentiating factor, B cell growth factor II and T cell-replacing factor (TRF). It can increase production and mobilization of eosinophils and CD34+ progenitors from the bone marrow. IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.Recombinant Human Interleukin-5 (rhIL-5) produced in E.coli is a disulfide-linked homodimer containing two non-glycosylated polypeptide chains of 116 amino acids each. A fully biologically active molecule, rhIL-5 has a molecular mass of 26.5 kDa analyzed by non-reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript. |
Form/Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
MW | 26.5 kDa, observed by non-reducing SDS-PAGE. |
Protein Sequence | MIPTEIPTS ALVKETLALL STHRTLLIAN ETLRIPVPVH KNHQLCTEEI FQGIGTLESQ TVQGGTVERL FKNLSLIKKY IDGQKKKCGE ERRRVNQFLD YLQEFLGVMN TEWIIES |
Source | Escherichia coli. |
Biological Activity | ED50 1.0× 10ˆ6 units/mg. |
Endotoxins | < 0.2 EU/μg, determined by LAL method. |
Storage | Lyophilized recombinant Human Interleukin-5 (rhIL-5) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIL-5 should be stable up to 2 weeks at 4°C or up to 3 months at -20°C. |
Buffer/Preservatives | Lyophilized after extensive dialysis against 25mM Tris, pH 8.0. |
Alternative names | Interleukin-5, IL5 Read more... |
Note | For research use only |
Application notes | Reconstituted in ddH2O at 100 μg/ml. |
Expiration Date | 6 months from date of receipt. |
> 98% as determined by SDS-PAGE and HPLC. | |
13.3 kDa | |
E.Coli |
Greater than 95% as determined by SDS-PAGE. | |
14.2 kDa | |
Mammalian cell |
ELISA, MS, SDS-PAGE, WB | |
Greater than 95% as determined by reducing SDS-PAGE. | |
Human cells |
ELISA, MS, SDS-PAGE, WB | |
Greater than 95% as determined by reducing SDS-PAGE. | |
Human cells |
Unconjugated | |
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 13.94 kDa after removal of the signal peptide.The apparent molecular mass of IL5-His is approximately 15-25 kDa due to glycosylation. | |
Mammalian |
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