Analytical Data
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Gene name
Siglec-2/CD22
- Application
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Alternative Names
B-lymphocyte cell adhesion molecule (BL-CAM) (Sialic acid-binding Ig-like lectin 2) (Siglec-2) (T-cell surface antigen Leu-14) (CD22)
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Species
Human
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Source
HEK293
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Tag
C- His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P20273
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Expression Region
20-687aa
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Molecular Weight
77.9 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
Related Products
Protein Description
Siglec-2, also known as CD22, is a member of the Sialic Acid Binding Immunoglobulin-like Lectins (Siglecs) family, which plays a crucial role in regulating B-cell activation and function. CD22 is predominantly expressed on B cells and serves primarily as an inhibitory receptor that modulates immune responses. Research has shown that Siglec-2/CD22 binding to sialic acid-containing glycoproteins can negatively regulate B cell receptor (BCR) signaling, thereby preventing excessive activation and autoimmunity. The therapeutic potential of targeting CD22 has gained interest, particularly in the context of B-cell malignancies such as acute lymphoblastic leukemia (ALL) and B-cell lymphoma. The development of CD22-targeted immunotherapies, including antibody-drug conjugates and CAR T-cell therapies, demonstrates promising efficacy in clinical settings. Consequently, the generation of recombinant CD22 protein is essential for further elucidating its structural and functional properties, as well as for the development of novel therapeutic strategies. Understanding the interactions between CD22 and its ligands at the molecular level can provide insights into the mechanisms of B cell regulation and pave the way for innovative treatments for B-cell disorders.
