货号 | MAB19681-SP |
别名 | 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; SIGLEC-2; SIGLEC2FLJ22814; T-cell surface antigen Leu-14 | 全称 | Sialic Acid Binding Ig-like Lectin 2 |
反应种属 | Human |
应用 | Western Blot(0.2 µg/mL) |
目标/特异性 | Detects human Siglec-2/CD22 in direct ELISAs and Western blots. In Western blots, approximately 25%cross-reactivity with recombinant human (rh) Siglec-7 and rhSiglec-9 isobserved, and no cross-reactivity with rhSiglec-3 is observed. |
使用方法 | Western Blot: 0.2 µg/mL |
来源 | Sterile PBS to a final concentration of 0.5 mg/mL. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 933 (Human); 12483 (Mouse) |
纯化方式 | Protein A or G purified from hybridoma culture supernatant |
免疫原 | Mouse myeloma cell line NS0-derived recombinant human Siglec-2/CD22 Asp20-Arg687 Accession # CAA42006 |
生物活性 | Human |
标记 | Unconjugated |
溶解方法 | Sterile PBS to a final concentration of 0.5 mg/mL. |
背景 | 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). |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
|
Detection of Human Siglec‑2/CD22 by Western Blot. Western blot shows lysates of Daudi human Burkitts lymphoma cell line. PVDF membrane was probed with 0.2 µg/mL of Mouse Anti-Human Siglec‑2/CD22 Monoclonal Antibody (Catalog # MAB19681) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for Siglec‑2/CD22 at approximately 140 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1. |