Analytical Data
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Gene name
SIGLEC14
- Application
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Alternative Names
SIGLEC14；Sialic acid-binding Ig-like lectin 14
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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
Q08ET2
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Expression Region
1-396aa
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AA Sequence
MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQVKRQGAQVTTERTVQLNVSYAPQNLAISIFFRNGTGTALRILSNGMSVPIQEGQSLFLACTVDSNPPASLSWFREGKALNPSQTSMSGTLELPNIGAREGGEFTCRVQHPLGSQHLSFILSVQRSSSSCICVTEKQQGSWPLVLTLIRGALMGAGFLLTYGLTWIYYTRCGGPQQSRAERPG
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Molecular Weight
43.9 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-14 is a type of sialic acid-binding immunoglobulin-like lectin primarily expressed on the surface of immune cells. It plays a critical role in regulating immune responses, particularly in the context of infections and inflammation. As an inhibitory receptor, Siglec-14 interacts with sialylated glycoconjugates on pathogens and host tissues, modulating cellular signaling pathways and potentially impacting the function of macrophages and other immune cells. Research into recombinant Siglec-14 proteins has gained traction as scientists seek to explore its binding properties, functional mechanisms, and potential therapeutic applications. This area of study is particularly relevant in the context of diseases where the immune system is dysregulated, such as cancer and autoimmune disorders. By expressing and purifying recombinant Siglec-14, researchers can investigate its interactions with various sialylated ligands, elucidate its role in immune modulation, and potentially develop targeted treatments that harness or inhibit its activity. Furthermore, understanding the structure-function relationship of Siglec-14 can pave the way for novel approaches in vaccine design and immunotherapy. Overall, the study of recombinant Siglec-14 proteins offers valuable insights into immune regulation and may contribute to the development of innovative therapeutic strategies.
