Microsize antibodies for $99 | Learn More >>

Monoclonal Antibody Flow Cytometry Manganese Ion Binding

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

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Arginase-1 (D4E3M™) XP® Rabbit mAb #93668.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

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

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

Background: The α isoform of protein phosphatase 2C (PP2C-α) is the catalytic subunit of a widely expressed serine/threonine phosphatase involved in regulation of the cell stress response (1,2). Also known as magnesium-dependent protein phosphatase (PPM1A), this monomeric phosphatase is a member of a conserved group of proteins that acts on many different substrates in numerous pathways. PP2C-α inhibits p38 MAPK and SAPK/JNK pathways activated in response to cell stress as seen in both in vivo and in vitro studies. Specifically, PP2C-α removes phosphates from MKK3 and MKK7, reducing activity of both proteins and inhibiting activation of the downstream kinases JNK and p38 MAPK, respectively (3). Another PP2C-α substrate is IKKβ, the critical regulator of NF-κB signaling. Dephosphorylation of IKKβ at Ser177/181 by PPM1A and PPM1B results in inactivation of IKKβ and inhibition of NF-κB signaling (4). PP2C-α is one of the phosphatases responsible for removing phosphate residues from cyclin dependent protein kinases. In a study using HeLa cell extracts, PP2C-α dephospohrylates CDK2 and CDK6, with a preference toward interacting with CDK2 phosphorylated at Thr160, a residue found in the activating T-loop of the kinase. Removal of phosphates from this site is thought to inactivate cyclin-associated kinases (5). PP2C-α induces cell cycle arrest and apoptosis, likely through activation of p53 though other pathways may also contribute to PP2C-α mediated cell death (6). Additional PP2C-α substrates include the Wnt signaling pathway protein axin (7) and CFTR, a chloride channel protein implicated in cystic fibrosis (8).