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Monoclonal Antibody Flow Cytometry Cell Recognition

Also showing Monoclonal Antibody Flow Cytometry Cell-Cell Recognition

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Dectin-1 is a C-type lectin receptor expressed by macrophages, monocytes, dendrtic cells, neutrophils, and a subset of γδ T cells (1,2). Dectin-1 is a glycoprotein with eight different isoforms, generated through alternative splicing (3-5). It plays an important role in anti-fungal immunity by acting as a pattern recognition receptor for β-glucans found on the cell wall of fungi and some bacteria (5,6). Dectin-1 is composed of a short amino-terminal cytoplasmic domain containing an ITAM-like motif, a transmembrane domain, and an extracellular carboxy-terminal C-type lectin domain (5). Dectin-1 recognizes β-glucans through its C-type lectin domain and transduces signals through its ITAM-like motif by recruiting and activating Syk (7,8). Dendritic cells activated through Dectin-1 promote differentiation of Th17 cells by producing IL-6 and IL-23 (9).

$305
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 Dectin-1 (E1X3Z) Rabbit mAb #60128.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Dectin-1 is a C-type lectin receptor expressed by macrophages, monocytes, dendrtic cells, neutrophils, and a subset of γδ T cells (1,2). Dectin-1 is a glycoprotein with eight different isoforms, generated through alternative splicing (3-5). It plays an important role in anti-fungal immunity by acting as a pattern recognition receptor for β-glucans found on the cell wall of fungi and some bacteria (5,6). Dectin-1 is composed of a short amino-terminal cytoplasmic domain containing an ITAM-like motif, a transmembrane domain, and an extracellular carboxy-terminal C-type lectin domain (5). Dectin-1 recognizes β-glucans through its C-type lectin domain and transduces signals through its ITAM-like motif by recruiting and activating Syk (7,8). Dendritic cells activated through Dectin-1 promote differentiation of Th17 cells by producing IL-6 and IL-23 (9).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: CD200 (OX2) and CD200R (OX2R) are membrane glycoprotein members of the Ig superfamily (1-3). CD200 is expressed by a range of cells, including neurons, epithelial cells, endothelial cells, fibroblasts, and lymphoid cells, while its receptor, CD200R, is found on myeloid and T cells (1-5). Interaction between CD200 and CD200R downregulates macrophage function and plays a role in immunosuppression and regulation of anti-tumor immune responses (3-7).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) (1,2). DUBs are categorized into 5 subfamilies: USP, UCH, OTU, MJD, and JAMM. UCHL1, UCHL3, UCHL5/UCH37, and BRCA-1-associated protein-1 (BAP1) belong to the ubiquitin carboxy-terminal hydrolase (UCH) family of DUBs, which all possess a conserved catalytic UCH domain of about 230 amino acids. UCHL5 and BAP1 have unique, extended carboxy-terminal tails. UCHL1 is abundantly expressed in neuronal tissues and testes, while UCHL3 expression is more widely distributed (3,4). Although UCHL1 and UCHL3 are the most closely related UCH family members with about 53% identity, their biochemical properties differ in that UCHL1 binds monoubiquitin and UCHL3 shows dual specificity toward both ubiquitin (Ub) and NEDD8, a Ub-like molecule.UCHL1 (PGP 9.5/PARK5) functions as a deubiquitinating enzyme and monoubiquitin stabilizer. In vitro studies have demonstrated that UCHL1 can hydrolyze isopeptide bonds between the carboxy-terminal glycine of Ub and the ε-amino group of lysine on target proteins. UCHL1 is also involved in the cotranslational processing of pro-ubiquitin and ribosomal proteins translated as ubiquitin fusions (5-7). Mice deficient in UCHL1 experience spasticity, suggesting that UCHL1 activity is required for the normal neuromuscular junction structure and function (5-7). Research studies have described loss of UCHL1 expression in numerous human malignancies, such as prostate, colorectal, renal, and breast carcinomas. Investigators have shown that loss of UCHL1 expression in breast carcinomas can be attributed to hyper-methylation of the UCHL1 gene promoter (8). While loss of UCHL1 expression is implicated in human carcinogenesis, mutation of UCHL1 has been implicated in neurodegenerative diseases such as Parkinson's and Alzheimer's (6,7).