| Code | CSB-YP013246HU |
| Abbreviation | Recombinant Human LY6G6D protein (Active) |
| MSDS | |
| Size | $250 |
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LY6G6D has emerged as a notable immunological target due to its selective expression on differentiated myeloid lineage cells, making it relevant to studies of tumor microenvironment biology and immune cell phenotyping. This recombinant human LY6G6D, covering the full-length mature protein (aa 20–104) with an N-terminal 6xHis tag, demonstrates robust binding activity validated by functional ELISA, where immobilized protein at 2 μg/mL bound anti-LY6G6D recombinant antibody with an EC50 of 2.816–3.741 ng/mL — a range that supports use in antibody characterization, sandwich ELISA development, and receptor-ligand interaction screening. Expressed in yeast to support eukaryotic folding of its Ly6/uPAR domain while minimizing mammalian-derived contaminants, this protein satisfies the purity and endotoxin criteria typical for cell-based functional assays, with greater than 95% purity by SDS-PAGE and endotoxin levels below 1.0 EU/μg. These attributes provide a suitable basis for generating positive assay controls and for use as an immunogen in antibody development campaigns.
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Our questions are the following:
1)Both baculovirus and yeast expressed proteins are N-terminal His tagged. However we can only detect the His tag from the baculovirus expressed but not the yeast expressed. Were there any attempt try to remove the his tag?
2)My second question is that are these protein constructs designed as secretory soluble proteins? If so, what was the signal peptides used since the native signal peptides were removed?
3)Have there been any validation attempts to look at if the proteins are folded correctly, e.g. using LY6G6D antibodies? Was there any other product validation steps performed?