Analytical Data
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Gene name
SIGLEC5
- Application
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Alternative Names
SIGLEC5；CD33L2；OBBP2；Sialic acid-binding Ig-like lectin 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15389
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Expression Region
17-434aa
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AA Sequence
EKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEI PYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSY FFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSL PGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMK RQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALR LLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRA QHPLGFLQIFLNLSVYSLPQLLGPSCSWEAEGLHCRCSFRARPAPSLCWR LEEKPLEGNSSQGSFKVNSSSAGPWANSSLILHGGLSSDLKVSCKAWNIY GSQSGSVLLLQGRSNLGT
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Molecular Weight
73 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Siglec-5 is a member of the sialic acid-binding Ig-like lectin (Siglec) family, primarily expressed on immune cells such as macrophages and dendritic cells. It plays a crucial role in modulating immune responses and maintaining self-tolerance by interacting with sialylated ligands on cells. The study of Siglec-5 and its recombinant protein forms has gained attention due to its potential implications in various diseases, including autoimmune disorders, infections, and cancer. Research indicates that Siglec-5 can inhibit the activation of immune cells, thereby influencing inflammatory responses and the balance between tolerance and immunity. Recombinant Siglec-5 proteins are valuable tools for elucidating the mechanisms of action and interactions of this receptor, as well as for developing therapeutic strategies that target Siglec-5 pathways. By engineering and producing recombinant forms of Siglec-5, researchers aim to investigate its structure-function relationships, binding affinities to different sialylated ligands, and its role in modulating immune cell signaling. This research could lead to novel approaches in immunotherapy and provide insights into its role in immune regulation, ultimately contributing to the development of targeted treatments for various diseases. Understanding the biology of Siglec-5 through recombinant protein studies is a critical step toward leveraging its potential in medical applications.
