CD22 Human
Sf9, Baculovirus cells.
CD22 Molecule, CD22 Antigen, Sialic Acid-Binding Ig-Like Lectin 2, B-Lymphocyte Cell Adhesion Molecule, T-Cell Surface Antigen Leu-14, SIGLEC-2, SIGLEC2, BL-CAM, Sialic Acid Binding Ig-Like Lectin 2, B-Cell Receptor CD22.
Greater than 85.0% as determined by SDS-PAGE.
Description
CD22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 907 amino acids (20-687a.a.) and having a molecular mass of 102.1kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150KDa).
CD22 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
CD22, also called Sialic Acid-Binding Ig-Like Lectin 2, belongs to the immunoglobulin (Ig) superfamily. This protein is involved in B-cell to B-cell interactions and plays a role in positioning B-cells within lymphoid tissues. CD22 can act as a positive regulator through interactions with Src family tyrosine kinases and can also function as an inhibitory receptor by recruiting cytoplasmic phosphatases.
Produced in Sf9 Baculovirus cells, CD22 is a single, glycosylated polypeptide chain consisting of 907 amino acids (20-687a.a.). It has a molecular weight of 102.1 kDa. Note: On SDS-PAGE, the molecular size appears to be between 100-150 kDa.
This CD22 protein is expressed with a C-terminal 239 amino acid hIgG-His-tag and is purified using proprietary chromatographic methods.
This CD22 protein solution has a concentration of 0.25 mg/ml and contains 10% glycerol and Phosphate Buffered Saline (pH 7.4).
For long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended.
Avoid repeated freeze-thaw cycles.
Purity is greater than 85.0% as determined by SDS-PAGE analysis.
CD22 Molecule, CD22 Antigen, Sialic Acid-Binding Ig-Like Lectin 2, B-Lymphocyte Cell Adhesion Molecule, T-Cell Surface Antigen Leu-14, SIGLEC-2, SIGLEC2, BL-CAM, Sialic Acid Binding Ig-Like Lectin 2, B-Cell Receptor CD22.
Sf9, Baculovirus cells.
DSSKWVFEHP ETLYAWEGAC VWIPCTYRAL DGDLESFILF HNPEYNKNTS KFDGTRLYES TKDGKVPSEQ KRVQFLGDKN KNCTLSIHPV HLNDSGQLGL RMESKTEKWM ERIHLNVSER PFPPHIQLPP EIQESQEVTL TCLLNFSCYG YPIQLQWLLE GVPMRQAAVT STSLTIKSVF TRSELKFSPQ WSHHGKIVTC QLQDADGKFL SNDTVQLNVK HTPKLEIKVT PSDAIVREGD SVTMTCEVSS SNPEYTTVSW LKDGTSLKKQ NTFTLNLREV TKDQSGKYCC QVSNDVGPGR SEEVFLQVQY APEPSTVQIL HSPAVEGSQV EFLCMSLANP LPTNYTWYHN GKEMQGRTEE KVHIPKILPW HAGTYSCVAE NILGTGQRGP GAELDVQYPP KKVTTVIQNP MPIREGDTVT LSCNYNSSNP SVTRYEWKPH GAWEEPSLGV LKIQNVGWDN TTIACAACNS WCSWASPVAL NVQYAPRDVR VRKIKPLSEI HSGNSVSLQC DFSSSHPKEV QFFWEKNGRL LGKESQLNFD SISPEDAGSY SCWVNNSIGQ TASKAWTLEV LYAPRRLRVS MSPGDQVMEG KSATLTCESD ANPPVSHYTW FDWNNQSLPY HSQKLRLEPV KVQHSGAYWC QGTNSVGKGR SPLSTLTVYY SPETIGRRLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
Product Science Overview
CD22 is composed of an extracellular domain, a single transmembrane domain, and a cytoplasmic tail. The extracellular domain contains seven immunoglobulin-like domains, which are responsible for its binding to sialic acid-containing ligands . The cytoplasmic tail contains multiple tyrosine-based motifs that are involved in signal transduction .
CD22 is primarily expressed on the surface of mature B cells and is involved in modulating B-cell receptor (BCR) signaling. It acts as an inhibitory co-receptor that dampens BCR signaling, thereby preventing overactivation of B cells and maintaining immune homeostasis . Additionally, CD22 plays a role in B-cell adhesion and migration by interacting with other cell surface molecules .
Recombinant CD22 is produced using various expression systems, including mammalian cells, to ensure proper folding and post-translational modifications. The recombinant protein is often tagged with a polyhistidine tag (His tag) to facilitate purification and detection . It is commonly used in research to study B-cell biology, develop therapeutic antibodies, and investigate the role of CD22 in B-cell malignancies .
CD22 has emerged as an important target for monoclonal antibody (mAb)-based therapies for B-cell malignancies, including lymphomas and leukemias . Therapeutic antibodies targeting CD22 can induce B-cell depletion, thereby reducing the tumor burden and improving patient outcomes. Additionally, CD22-targeted therapies are being explored in the treatment of autoimmune diseases, where B-cell dysregulation plays a key role .
Recombinant CD22 is also used in various assays to study its binding interactions, signaling pathways, and functional roles in B cells. For example, it can be used in enzyme-linked immunosorbent assays (ELISAs) to measure the binding affinity of antibodies or other ligands to CD22 . Furthermore, recombinant CD22 is utilized in flow cytometry and immunohistochemistry to detect and quantify CD22 expression on B cells .
