Analytical Data
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Gene name
SIGLEC7
- Application
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Alternative Names
SIGLEC7；AIRM1；Sialic acid-binding Ig-like lectin 7
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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
Q9Y286
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Expression Region
19-353aa
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AA Sequence
QKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRA GNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDA GRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTC SVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQ VTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLE GQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEF TCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLL
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Molecular Weight
63 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-7, or sialic acid-binding immunoglobulin-like lectin 7, is a member of the Siglec family of proteins, which are known to play critical roles in immune regulation and cell signaling. It is predominantly expressed on the surface of immune cells, particularly natural killer (NK) cells and certain myeloid cells, where it interacts with sialic acid-containing glycans on neighboring cells. This interaction can modulate immune responses, influencing processes such as cell activation, proliferation, and apoptosis. The study of Siglec-7 has gained significant attention due to its potential implications in various pathological conditions, including cancer and autoimmune diseases. In tumors, Siglec-7 expression can be upregulated, enabling malignant cells to evade immune surveillance by dampening responses from NK cells. Consequently, researchers have been investigating the production and characterization of recombinant Siglec-7 proteins to understand its structural features and ligand-binding properties better. These studies aim to elucidate the role of Siglec-7 in immune evasion and establish its potential as a therapeutic target. Recombinant Siglec-7 proteins can be utilized in assays to screen for small molecules or antibodies that can block its interactions with sialylated ligands, potentially enhancing antitumor immunity. Overall, research into recombinant Siglec-7 is pivotal for developing novel immunotherapeutic strategies that could improve outcomes in cancer treatment and other diseases associated with immune dysregulation.
