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Monoclonal Antibody Flow Cytometry Peptide Antigen Transport

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated DC-SIGN (D7F5C) XP® Rabbit mAb #13193.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: DC-SIGN (CD209, CLEC4L) is a C-type lectin receptor expressed by dendritic cells (DCs) (1,2). The DC-SIGN transcript can undergo several splicing events to generate at least thirteen different transmembrane and soluble isoforms (3). DC-SIGN responds to a broad range of pathogens due to its ability to recognize both mannose and fructose carbohydrates, and is well studied for its role in HIV infection. Recognition of the HIV envelope glycoprotein gp120 by DC-SIGN leads to internalization of HIV by DCs and facilitates transmission of the virus to CD4+ T cells (2,4). DC-SIGN also mediates adhesion to T cells through interaction with ICAM-3, as well as transmigration across the endothelium by binding to ICAM-2 (1,5). The DC-SIGN receptor can modulate TLR signaling by activating the kinase Raf-1 (6,7). The closely related molecule DC-SIGNR (L-SIGN, CLEC4M) is 77% homologous to DC-SIGN and likely arose through a gene duplication event (8). Like DC-SIGN, DC-SIGNR binds mannose carbohydrates on the surface of pathogens (8,9). However, the expression patterns of the two receptors differ, as DC-SIGNR expression is restricted to endothelial cells of the liver, lymph node, and placenta (10). Murine cells contain a set of related molecules, SIGNR1-SIGNR8 (11). Based on sequence analysis, there is no clear murine ortholog to human DC-SIGN, however SIGNR3 is the most functionally similar due to its ability to recognize both mannose and fructose structures (11).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: DC-SIGN (CD209, CLEC4L) is a C-type lectin receptor expressed by dendritic cells (DCs) (1,2). The DC-SIGN transcript can undergo several splicing events to generate at least thirteen different transmembrane and soluble isoforms (3). DC-SIGN responds to a broad range of pathogens due to its ability to recognize both mannose and fructose carbohydrates, and is well studied for its role in HIV infection. Recognition of the HIV envelope glycoprotein gp120 by DC-SIGN leads to internalization of HIV by DCs and facilitates transmission of the virus to CD4+ T cells (2,4). DC-SIGN also mediates adhesion to T cells through interaction with ICAM-3, as well as transmigration across the endothelium by binding to ICAM-2 (1,5). The DC-SIGN receptor can modulate TLR signaling by activating the kinase Raf-1 (6,7). The closely related molecule DC-SIGNR (L-SIGN, CLEC4M) is 77% homologous to DC-SIGN and likely arose through a gene duplication event (8). Like DC-SIGN, DC-SIGNR binds mannose carbohydrates on the surface of pathogens (8,9). However, the expression patterns of the two receptors differ, as DC-SIGNR expression is restricted to endothelial cells of the liver, lymph node, and placenta (10). Murine cells contain a set of related molecules, SIGNR1-SIGNR8 (11). Based on sequence analysis, there is no clear murine ortholog to human DC-SIGN, however SIGNR3 is the most functionally similar due to its ability to recognize both mannose and fructose structures (11).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: CD74, which is also known as the MHC Class II-associated invariant chain (Ii), is a type II transmembrane glycoprotein that plays a critical role in the antigen presentation process as a chaperone of MHC Class II proteins. It is expressed at high levels on B cells and to a lesser extent on numerous antigen presenting cell (APC) types including dendritic cells, Langerhans cells, monocytes, and macrophages as well as non-traditional APCs such as epithelial cells (1,2). CD74 was initially identified for its ability to regulate the folding and intracellular trafficking of newly synthesized MHC Class II molecules. Following expression, CD74 self-assembles as a trimer that serves as a scaffold for the assembly of MHC Class II molecules. Through this interaction, CD74 blocks the peptide binding cleft of MHC Class II molecules and prevents their premature association with endogenous polypeptides (3). Binding to CD74 also facilitates the translocation of MHC Class II molecules from the endoplasmic reticulum to the endocytic compartments during antigen presentation (4). In addition to its role as an MHC Class II chaperone, CD74 is also the receptor for macrophage migration-inhibitory factor (MIF). Binding to CD74 and its co-receptor, CD44, has been shown to induce the activation of the NFkB and ERK pathways to promote cell proliferation and survival signals (5,6). Recent studies have identified CXCR2 and CXCR4 as co-receptors for CD74 where MIF binding to CD74 complexes contributes to MIF-mediated monocyte chemotaxis and the induction of Akt signaling, respectively (7,8). Increased CD74 surface expression has been reported under inflammatory conditions and in certain types of cancer cells implying a potential role in tumorigenesis (9).