Biotin-conjugated recombinant human Siglec-9 with a C-terminal His-tag, derived from the transfected human HEK293 cells.
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Figure 1. Deglycosylation analysis of purified recombinant proteins. Lane 1, protein ladder (kDa). Lane 2, glycosylated protein (delivered to customers). Lanes 3 and 4, deglycosylated proteins under native and denature conditions respectively.
| Size | 50 µg |
| Estimated Lead Time | 1-2 business days |
| Species | Human |
| Accession Number | Q9Y336 |
| Gene Symbols | SIGLEC9 |
| Protein Name / Synonyms | Sialic acid-binding Ig-like lectin 9, Siglec-9, CDw329, Protein FOAP-9, CD329. |
| Expressed Region | Met25-Gly348 |
| Expression System | HEK293 cells |
| Conjugation | Biotin |
| Tag | C-terminal histidine tag. The primary amino groups (-NH2) at the N-terminus and the side chains of lysine (K) residues were biotin-conjugated using the standard chemical labeling method. |
| Purity | >90% |
| Purity Determined By | SDS-PAGE under reducing conditions and visualized by Coomassie blue staining |
| Molecular Weight (kDa) | Recombinant protein product has a calculated molecular mass of 35 kDa. Due to the abundant glycosylation, it migrates as approximately 55-60 kDa major protein bands in SDS-PAGE under DTT, beta-mercaptoethanol reducing conditions. See deglycosylation analysis image below. |
| Format | Lyophilized powder |
| Formulation | Lyophilized from a 0.2 µm filtered solution in PBS (pH 7.4) |
| Concentration (lot specific) | Determined by Pierce BCA protein assay |
| Reconstitution | Briefly spin the vial and bring the contents to the bottom prior to opening. It is recommended to reconstitute at 0.5 - 1.0 mg/mL with sterile deionized water. |
| Endotoxin Level | <0.5 EU per µg of the protein as determined by the LAL method |
| Shipping Type | Ambient temperature |
| Storage | -20°C |

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Figure 1. Deglycosylation analysis of purified recombinant proteins. Lane 1, protein ladder (kDa). Lane 2, glycosylated protein (delivered to customers). Lanes 3 and 4, deglycosylated proteins under native and denature conditions respectively.