Recombinant Human B-Cell Receptor Cd22 (CD22) Protein (His-SUMO)

Name: Recombinant Human B-Cell Receptor Cd22 (CD22) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10974P
Price: 418.4 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Car-nk targets proteins, Car-t cell therapy targets, Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

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Product Overview

Description	Recombinant Human B-Cell Receptor Cd22 (CD22) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P20273
Target Symbol	CD22
Synonyms	B cell receptor CD22 precursor; B lymphocyte cell adhesion molecule; B-cell receptor CD22; B-lymphocyte cell adhesion molecule; BL CAM; BL-CAM; BLCAM; CD 22; CD22; CD22 antigen; CD22 molecule; CD22 protein; CD22_HUMAN; Lectin 2; Leu14; Lyb8; MGC130020; sialic acid binding Ig like lectin 2; Sialic acid binding immunoglobulin like lectin 2; Sialic acid-binding Ig-like lectin 2; SIGLEC 2; Siglec-2; SIGLEC2; T cell surface antigen Leu 14; T-cell surface antigen Leu-14
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPL
Expression Range	553-672aa
Protein Length	Partial
Mol. Weight	26.3 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Protein Families	Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
Database References	HGNC: 1643 OMIM: 107266 KEGG: hsa:933 STRING: 9606.ENSP00000085219 UniGene: Hs.579691
Tissue Specificity	B-lymphocytes.

Gene Functions References

Conjugates of these multivalent ligands with auristatin and saporin toxins are efficiently internalized via hCD22 resulting in killing of B-cell lymphoma cells PMID: 28829594
This is the first time a NMR-based binding study of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt's lymphoma Daudi cells has been described. PMID: 27808110
Here the authors structurally characterize the ectodomain of CD22 and present its crystal structure with the bound therapeutic antibody epratuzumab, which gives insights into the mechanism of inhibition of B-cell activation. PMID: 28970495
hCD22 transgenic mice develop normal humoral responses in a peanut allergy oral sensitization model. Homing of B cells to Peyer's patches was partially rescued by expression of hCD22 compared with CD22(-/-) B cells, although not to wild-type levels. PMID: 28972089
Diabody-based (177)Lu-radioimmunoconjugate for CD22-directed radioimmunotherapy reduced disease burden in a non-Hodgkin lymphoma mouse model. PMID: 27524505
Siglec-1 and Siglec-2 are potential biomarkers in autoimmune disease. (Review) PMID: 26752092
We aimed to screen exons 9-14 of the CD22 gene, which is a mutational hot spot region in B-precursor acute lymphoblastic leukemia (pre-B ALL) patients. Nine variants, of which two novel, were found. Novel variants were in introns 10 and 13. Gly745Asp (rs10406069) variant was missense and Cys790Arg (rs79438722) variant was silent. PMID: 27486888
Anti-CD22-magnetic nanoparticles-doxorubicin inhibited the proliferation of Raji cells, significantly increased the uptake of doxorubicin, and induced apoptosis. PMID: 26379425
results demonstrate that loss of high affinity CD22 ligands on GC B-cells occurs in both mice and humans through alternative mechanisms, unmasking CD22 relative to naive and memory B-cells PMID: 26507663
MicroRNA-19a and CD22 Comprise a Feedback Loop for B Cell Response in Sepsis. PMID: 26017478
These results suggest that the in vivo mechanism of non-ligand-blocking epratuzumab may, in part, involve the unmasking of CD22 to facilitate the trans-interaction of B cells with vascular endothelium. PMID: 25484043
By using integrative genomics and analysing the relationships of COPD phenotypes with SNPs and gene expression in lung tissue, we identified CST3 and CD22 as potential causal genes for airflow obstruction. PMID: 25182044
study detected the expression of CD22 and CD72 on B cells of myasthenia gravis, compared to multiple sclerosis patient controls and healthy controls y PMID: 23184497
In the absence of functional CD22, B cells have a "hyperactivated" phenotype, CD22 dysfunction could contribute to the pathogenesis of autoimmune diseases. (Review) PMID: 23083346
The finding that CD22 is expressed on lung cancer cells is significant in revealing a heretofore unknown mechanism of tumorigenesis and metastasis PMID: 22986740
Anti-CD22 recombinant immunotoxin moxetumomab pasudotox has activity in relapsed/refractory hairy cell leukemia. PMID: 22355053
Our study implicates the CD22DeltaE12 genetic defect in the aggressive biology of relapsed or therapy-refractory paediatric B-lineage ALL. PMID: 22017452
This CD22-targeted polymer carrier may be useful for siRNA delivery to lymphoma cells. PMID: 21629223
Taken together, these results suggest that negative regulation of TLR signaling of B cells is an intrinsic property of CD22. PMID: 21178327
The efficacy of a ligand-targeting approach to B cell-specific depletion therapy for cancer may be the ability of CD22 to recycle and accumulate ligand-decorated cargo intracellularly, as an endocytic receptor. PMID: 21178016
These striking findings implicate CD22DeltaE12 as a previously undescribed pathogenic mechanism in human B-precursor leukemia. PMID: 20841423
B cell surface receptors CD20 and CD22 are significantly affected in patients with SLE, pointing to their possible involvement in the aetiopathogenesis of the disease and in the regulatory mechanisms in response to the immune disturbance. PMID: 20726320
The B-cell receptor IgM was found to be a major in situ trans ligand of CD22. PMID: 20172905
Data show that anti-CD22 autoantibodies were positive in 80% of TSK/+ mice and in 22% of SSc patients. PMID: 19919568
The Lyn/CD22/SHP-1 pathway is important in autoimmunity. Naive and tolerant B-cells differ in their calcium signaling in response to antigenic stimulation. PMID: 11826756
Disulfide bonds and the resulting 3D conformation of the CD22 molecules may have important roles in the difference of antigenicity of CD22 beta in B cells and basophils PMID: 11882357
ligand-binding of CD22 influences its intracellular signaling domain and is needed for inhibition of the B cell receptor signal PMID: 11994426
masking of the alpha2-6-linked sialic acid binding site of CD22 involves many cell surface sialoglycoproteins, without requiring specific ligand(s) and/or is mediated by secondary interactions with Sias on CD45 and sIgM PMID: 15240561
Aberrant CD22 expression is a useful marker for detection of monoclonal B cells admixed with numerous benign polyclonal B cells PMID: 15899772
decreased CD22 expression may be associated with the activation of B cells in Bullous pemphigoid (BP), but not associated with BP-specific antibody production PMID: 17055225
study showed that a synonymous SNP in CD22, c.2304C > A, was significantly associated with susceptibility to limited cutaneous systemic sclerosis PMID: 17493148
The results suggest that these two siglec proteins have evolved distinct endocytic mechanisms consistent with roles in cell signaling and innate immunity. PMID: 17562860
These results indicate that the alpha2-6-sialylated 6-sulfo-LacNAc determinant serves as an endogenous ligand for human CD22 and suggest the possibility that 6-GlcNAc sulfation as well as alpha2-6-sialylation may regulate Siglec-2 functions in humans. PMID: 17728258
SAP is inducibly expressed in the human BJAB cells, and co-localizes and interacts with CD22. SAP binding to the inhibitory immunoreceptor CD22 regulates calcium mobilization in B cells. PMID: 19150402

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.