Recombinant Human Siglec-2/CD22 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Siglec-2/CD22 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Kelm, S. et al. (1994) Current Biology 4:965. The ED50 for this effect is 0.03-0.15 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-2/CD22 protein
Human Siglec-2
(Asp20-Arg687)
Accession # CAA42006
DIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asp20
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
CD22
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
101.9 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
122-127 kDa, reducing conditions
Publications
Read Publications using
1968-SL in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Siglec-2/CD22 Fc Chimera Protein, CF

  • 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

Background

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).

  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.

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1968-SL
Species: Hu
Applications: Bioactivity

Publications for Siglec-2/CD22 (1968-SL)(4)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 2 applications: Bioassay, CAR-T (Flow Cytometry).


Filter By Application
Bioassay
(3)
CAR-T (Flow Cytometry)
(1)
All Applications
Filter By Species
Human
(4)
All Species
Showing Publications 1 - 4 of 4.
Publications using 1968-SL Applications Species
TJ Fry, NN Shah, RJ Orentas, M Stetler-St, CM Yuan, S Ramakrishn, P Wolters, S Martin, C Delbrook, B Yates, H Shalabi, TJ Fountaine, JF Shern, RG Majzner, DF Stroncek, M Sabatino, Y Feng, DS Dimitrov, L Zhang, S Nguyen, H Qin, B Dropulic, DW Lee, CL Mackall CD22-targeted CAR T cells induce remission in B-ALL that is naive or resistant to CD19-targeted CAR immunotherapy Nat. Med., 2018;24(1):20-28. 2018 [PMID: 29155426] (CAR-T (Flow Cytometry), Human) CAR-T (Flow Cytometry) Human
Chen, Guo-Yun, Brown, Nicholas, Wu, Wei, Khedri, Zahra, Yu, Hai, Chen, Xi, van de Vlekkert, Diantha, D'Azzo, Alessand, Zheng, Pan, Liu, Yang Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1. Elife, 2014;3(0):e04066. 2014 [PMID: 25187624] (Bioassay, Human) Bioassay Human
Haso W, Lee D, Shah N, Stetler-Stevenson M, Yuan C, Pastan I, Dimitrov D, Morgan R, Fitzgerald D, Barrett D, Wayne A, Mackall C, Orentas R Anti-CD22-chimeric antigen receptors targeting B-cell precursor acute lymphoblastic leukemia. Blood, 2013;121(7):1165-74. 2013 [PMID: 23243285] (Bioassay, Human) Bioassay Human
Kwong KY, Baskar S, Zhang H, Mackall CL, Rader C Generation, affinity maturation, and characterization of a human anti-human NKG2D monoclonal antibody with dual antagonistic and agonistic activity. J. Mol. Biol., 2008;384(5):1143-56. 2008 [PMID: 18809410] (Bioassay, Human) Bioassay Human

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FAQs for Siglec-2/CD22 (1968-SL). (Showing 1 - 1 of 1 FAQs).

  1. I am interested in buying a CD22 antibody for fluorescence microscopy and FACS I red on your web page that you also offer to label your antibodies, if required, is that correct?
    • We do have the ability to perform custom conjugations on certain antibodies, including some to the CD22 protein. If you send me the conjugate you are interested in I can provide you with a quote.

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Bioinformatics

Gene Symbol CD22
Uniprot