Flow Cytometry: CD2 Antibody (12-15) [NBP1-26666] - BALB/c mouse splenocytes were stained with Rat Anti-Mouse CD2-UNLBfollowed by Mouse Anti-Rat IgG1-FITC.
Flow Cytometry: CD2 Antibody (12-15) [NBP1-26666] - Analysis using the Biotin conjugate of NBP1-26666. Multiple staining of C57BL/6 splenocytes.
Flow Cytometry: CD2 Antibody (12-15) [NBP1-26666] - Analysis using the FITC conjugate of NBP1-26666. Staining of 1 ug/1^6 BALB/c lymph node cells with rat anti-mouse CD2-FITC. Lymphocytes were then gated and analyzed by ...read more
Flow Cytometry: CD2 Antibody (12-15) [NBP1-26666] - Analysis using the FITC conjugate of NBP1-26666. Staining of C57BL/6 mouse splenocytes with NBP1-26669 (PE conjugate) and NBP1-26667 (FITC conjugate).
Flow Cytometry: CD2 Antibody (12-15) [NBP1-26666] - BALB/c mouse splenocytes were stained with Rat Anti-Mouse CD2-FITC (NBP1-26667).
Alternate Names for CD2 Antibody (12-15) - Azide and BSA Free
CD2 antigen (p50), sheep red blood cell receptor
CD2 antigen
CD2 molecule
CD2
Erythrocyte receptor
FLJ46032
Leu-5
LFA-2
LFA-3 receptor
Ly37
lymphocyte-function antigen-2
Rosette receptor
SRBC
SRBC-R
T11
T-cell surface antigen CD2
T-cell surface antigen T11/Leu-5
Background
CD2, also known as sheep red blood cell receptor (SRBC-R), erythrocyte receptor, LFA-2, and T11, is a type I transmembrane glycoprotein that is expressed on the surface of T cells, natural killer (NK) cells, thymocytes, and dendritic cells (1,2). CD2 is a member of the immunoglobulin (Ig) superfamily and a costimulatory receptor that functions in formation of the immunological synapse and T cell activation and signaling (1). The human CD2 protein is 351 amino acids in length with a theoretical molecular weight of ~40 kDa, but a fully glycosylated protein can weight closer to 50 kDa (1,3). The CD2 protein contains a signal sequence, an extracellular domain (ECD) composed of an Ig-like V-type domain followed by an Ig-like C-type domain, a transmembrane helical domain, and a proline-rich cytoplasmic tail (1,3). CD2 binds with CD58, also called LFA-3, which is a surface glycoprotein expressed by antigen presenting cells (APCs) and other target cells (1,2). While CD58 is the primary ligand for CD2 in humans, it also interacts with CD59 and CD48, albeit with lower affinity (1,2). However, in mice and rats which lack CD58 the main ligand for CD2 is CD48 (4). Research has found that when there is no direct interaction, CD2 co-immunoprecipitates with the T cell receptor (TCR)/CD3 complex (1). CD2 is an adhesion molecule with a variety of functions including actin cytoskeleton rearrangement, immunological synapse formation through T cell-APC binding, thymocyte development and T cell activation, and NK cell activation (1,2). The immunological synapse forms upon T cell-APC engagement and creates a contact zone of supramolecule activation clusters (SMACs) where CD2-CD58 is part of the central SMAC (cSMAC) (2).
The CD2-CD58 interaction has been shown to play a role in anti-tumor immune response, where reduced CD58 signaling is associated with immune escape of tumor cells in various hematological and lymphoid malignancies, but restoration of the signal promotes an anti-tumor response (2,5). Additionally, following cytomegalovirus (CMV) infection, CD2's binding to upregulated CD58 on CMV-infected cells is crucial for the activation and function of adaptive NK cells in the anti-viral response (2). In contrast, in situations where there is an increase in T cell and NK cell activation, like various autoimmune disorders or following organ transplant, costimulatory blockade of CD2-CD58 may be a potential therapeutic treatment approach (1). Mouse and rat xenograft models have shown that blocking the CD2 using anti-CD2 monoclonal antibodies contributes to graft survival and protects against lymphocyte infiltration and inflammatory damage (2).
References
1. Binder C, Cvetkovski F, Sellberg F, et al. CD2 Immunobiology. Front Immunol. 2020;11:1090. https://doi.org/10.3389/fimmu.2020.01090
2. Zhang Y, Liu Q, Yang S, Liao Q. CD58 Immunobiology at a Glance. Front Immunol. 2021;12:705260. https://doi.org/10.3389/fimmu.2021.705260
3. Uniprot (P06729)
4. van der Merwe PA. A subtle role for CD2 in T cell antigen recognition. J Exp Med. 1999;190(10):1371-1374. https://doi.org/10.1084/jem.190.10.1371
5. Nishikori M, Kitawaki T, Tashima M, Shimazu Y, Mori M, et al. Diminished CD2 Expression in T cells Permits Tumor Immune Escape. J Clin Cell Immunol. 2016;7:406. https://doi.org/10.4172/2155-9899.1000406
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
FAQs for CD2 Antibody (NBP1-26666). (Showing 1 - 1 of 1 FAQs).
Does this antibody cross react with the FC receptor?
The answer to your question is likely to be "NO", this antibody should not be cross reactive with the mouse FC receptors, based on the following reasons: 1) Since we do not map the epitopes of our antibodies and the immunogen sequence of this antibody is the proprietary information, I think it is safe to say that the extracellular domain (a.a. 32 - 302 on Uniprot) of the mouse CD2 protein contains the epitope, where NBP1-26666 interacts with. Based on this assumption, I have done an a.a. sequence comparison. 2) There are several different types of Fc receptors (FcR) and the major ones are those binding to IgG, which are called Fc-gamma receptors (Fc gamma R). Fc gamma R belongs to the immunoglobulin superfamily and includes several members, Fc gamma RI (CD64), Fc gamma RIIA (CD32), Fc gamma RIIB (CD32), etc., which differ in their antibody affinities due to their different molecular structure. Therefore the a.a. sequences derived from mouse CD64 and CD32 were compared with the sequence of mouse CD2 at the a.a. 32 - 302.
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