Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate

Fc Chimera
Catalog # Availability Size / Price Qty
ATJ1968-050
Detection of Human Siglec-2/CD22 Antibody with Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate by Flow Cytometry.
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Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate Summary

Product Specifications

Purity
>80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by flow cytometry for its ability to bind anti-Human Siglec-2/CD22 Monoclonal Antibody conjugated fluorescent beads.
Source
Mouse myeloma cell line, NS0-derived human Siglec-2/CD22 protein
 Human Siglec-2/CD22
(Asp20-Arg687)
Accession # CAA42006.1
DIEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Analysis
Asp20
Structure / Form
Disulfide-linked homodimer labeled with Atto 488 via amines
Excitation Wavelength: 501 nm
Emission Wavelengh: 523 nm
Predicted Molecular Mass
101.9 kDa (monomer)
SDS-PAGE
114-126 kDa, under reducing conditions

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ATJ1968

ATJ1968

Formulation Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Data Images

Flow Cytometry Detection of Human Siglec-2/CD22 Antibody with Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate by Flow Cytometry. View Larger

Fluorescent beads conjugated to anti-Human Siglec 2/CD22 Monoclonal Antibody (MAB1968) were stained with (A) Recombinant Human Siglec 2/CD22 Protein, Atto 488 Conjugate (Catalog # ATJ1968) or (B) unstained.

SDS-PAGE Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate SDS-PAGE. View Larger

2 μg/lane of Recombinant Human Siglec-2/CD22 Protein, Atto 488 Conjugate (Catalog # ATJ1968) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 114-126 kDa adn 228-252 kDa, respectively.

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Background: Siglec-2/CD22

Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains (1, 2). Eleven human Siglecs have been cloned and characterized. They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and the identified Siglecs 5 to 11 (1 ‑ 3). To date, no Siglec has been shown to recognize any cell surface ligand other than sialic acid, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Human Siglec-2, also known as B‑cell antigen CD22 or B‑lymphocyte cell adhesion molecule (BL-CAM), is a B‑cell restricted glycoprotein that is expressed in the cytoplasm of progenitor B and pre-B cells and on the surface of mature B cells. Two distinct human Siglec-2/CD22 cDNAs that arise from differential RNA processing of the same gene have been isolated. The predominant Siglec-2/CD22 beta encodes an 847 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, six Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail with 4 immunoreceptor tyrosine-based inhibition motifs (ITIMs) (4). The variant Siglec-2/CD22 alpha encodes a 647 aa polypeptide missing two Ig-like C2-type domains and has a truncated (23 aa) cytoplasmic tail (5). Siglec-2/CD22 is an adhesion molecule that preferentially binds alpha 2,6- linked sialic acid on the same (cis) or adjacent (trans) cells. Interaction of CD22 with trans ligands on opposing cells was found to be favored over the binding of ligands in cis (9). Besides its role as an adhesion molecule, Siglec-2/CD22 is a coreceptor that physically interacts with B‑cell receptor (BCR) and is rapidly phosphorylated upon BCR ligation. It negatively regulates BCR signals by recruiting tyrosine phosphatase SHP-1 to its ITIMs. Phosphorylated Siglec-2/CD22 can also interact with other intracellular effector proteins such as Syk, PLC gamma, PI3 kinase and Grb-2, suggesting it may play a role in positive signaling (2, 7, 8).

References
  1. Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
  2. Crocker, P.R. and A. Varki (2001) Immunology 103:137.
  3. Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
  4. Wilson, G.L et al. (1991) J. Exp. Med. 173:137.
  5. Stamenkovic, I. and B. Seed (1990) Nature 345:74.
  6. Kelm, S. et al. (1994) Current Bio. 4:965.
  7. Ravetch, J.V. and L.L. Lanier (2000) Science 290:84.
  8. Wienands, Y.J. et al. (1999) J. Biol. Chem. 274:18769.
  9. Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. 101:6104.
Long Name
Sialic Acid Binding Ig-like Lectin 2
Entrez Gene IDs
933 (Human); 12483 (Mouse); 308501 (Rat); 102130968 (Cynomolgus Monkey)
Alternate Names
B-cell receptor CD22; BL-CAM; B-lymphocyte cell adhesion molecule; CD22 antigenMGC130020; CD22 molecule; CD22; sialic acid binding Ig-like lectin 2; Sialic acid-binding Ig-like lectin 2; Siglec2; Siglec-2; SIGLEC2FLJ22814; T-cell surface antigen Leu-14

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