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Product listing: HSP27 (E1J4D) Rabbit mAb (IHC Preferred), UniProt ID P04792 #50353 to IDH2 (KrMab-3) Mouse mAb, UniProt ID P48735 #60322

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: HSP40 and HSP40-like proteins represent a large family of chaperone proteins that are homologous to E. coli DnaJ protein (1). These proteins are classified into three subtypes based on their structures. The common feature of the family is a conserved J domain, which is usually located at the amino terminus of proteins and responsible for their association with HSP70 (1,2). Human HSP40, also known as Hdj1, belongs to subtype II that contain a unique Gly/Phe-rich region (2). HSP40 family proteins bind unfolded proteins, prevent their aggregation, and then deliver them to HSP70 (2,3). Another major function of HSP40 is to stimulate ATPase activity of HSP70, which causes conformational change of the unfolded proteins (4,5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 or components of the protein degradation machinery such as CHIP and BAG-1, which either leads to protein folding or degradation, respectively (6).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated HSP60 (D6F1) XP® Rabbit mAb #12165.
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Xenopus, Zebrafish

Application Methods: Western Blotting

Background: In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8).

$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 HSP60 (D6F1) XP® Rabbit mAb #12165.
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Xenopus, Zebrafish

Application Methods: Flow Cytometry

Background: In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Xenopus, Zebrafish

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

Background: In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated HSP90 (C45G5) Rabbit mAb #4877.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$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 HSP90 (C45G5) Rabbit mAb #4877.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Pig, Rat

Application Methods: Western Blotting

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

Background: HSPA8, alternately known as HSC70 or HSP73, is a constitutively expressed member of the HSP70 superfamily (1). Although its primary role in cells appears to be that of a general chaperone for unfolded proteins, HSPA8 has also been identified as the uncoating ATPase responsible for removing clathrin from coated vesicles and may also play a role in stabilizing untranslated mRNAs (1-5). In addition to these "housekeeping" functions, HSPA8 may also have an important role in inducible cellular stress responses. For example, oxidative or thermal stress promotes the nuclear/nucleolar accumulation of HSPA8, where it forms a complex with the topoisomerase I complex and likely protects it from heat inactivation (6,7). HSPA8 is reportedly phosphorylated in response to DNA damage, but it remains unclear what effect, if any, this has on HSPA8 function (8-10). Numerous high throughput studies support this observation. For more information, please see the HSPA8 page in PhosphoSitePlus® at www.phosphosite.org.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).

$345
100 µg
Neutralizing antibodies can be used to inhibit normal biological function through their binding to biological molecules. These reagents can be used to determine the effects that a particular molecule has in biological systems. Human EGF Neutralizing (D8A1) Rabbit mAb has been shown to neutralize the EGF-induced proliferation of MCF 10A cells in vitro with an ND50 in the range of 200-700 ng/ml.
REACTIVITY
Human
$345
100 µg
Neutralizing antibodies can be used to inhibit normal biological function through their binding to biological molecules. These reagents can be used to determine the effects that a particular molecule has in biological systems. Human IL-17A Neutralizing (D13C2) Rabbit mAb has been shown to neutralize the production of IL-6 from human dermal fibroblast cells in vitro with an ND50 in the range of 8-50 ng/ml.
REACTIVITY
Human
$345
100 µg
Neutralizing antibodies can be used to inhibit normal biological function through their binding to biological molecules. These reagents can be used to determine the effects that a particular molecule has in biological systems. Human IL-4 Neutralizing (D20H1) Rabbit mAb has been shown to neutralize the proliferation of TF-1 cells in vitro with an ND50 in the range of 3-19 ng/ml.
REACTIVITY
Human
$345
100 µg
Neutralizing antibodies can be used to inhibit normal biological function through their binding to biological molecules. These reagents can be used to determine the effects that a particular molecule has in biological systems. TNF-α has known functions of cell cytotoxicity, cell activation, and apoptosis in different cell types. Human TNF-α Neutralizing (D1B4) Rabbit mAb has been shown to neutralize the cytotoxic effects of TNF-α in L-929 mouse fibroblast cells. Utilizing 1 ng/ml of hTNF-α #8902 and 1 µg/ml of actinomycin D, Human TNF-α Neutralizing (D1B4) Rabbit mAb rescued L-929 cells with an ND50 in the range of 4-12 ng/ml.
REACTIVITY
Human

Background: TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk1/2, p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA damage resulting from genotoxic stress activates cellular checkpoints that prevent or delay cell division until damaged DNA is repaired or the cell follows an apoptotic pathway. The Rad9 homolog A (Rad9A, Rad9) protein is part of a checkpoint protein complex that acts as an early sensor of DNA damage. Together with the HUS1 and Rad1 checkpoint proteins, Rad9 forms a heterotrimeric 9-1-1 complex with a ring structure similar to the processivity factor PCNA. The 9-1-1 complex induces multiple signaling pathways, including the ATM- and ATR-activated DNA repair pathways (1,2). A functional 9-1-1 complex is required for ATR-dependent S phase checkpoint signaling (3).The 9-1-1 complex interacts with DNA topoisomerase 2-binding protein 1 (TopBP1) in response to DNA damage, activating ATR and causing signal amplification through further recruitment of TopBP1 (4). The 9-1-1 complex interacts with DNA mismatch repair proteins MSH2, MSH3, and MSH6 to play a role in mismatch repair (5). During an error-free DNA damage tolerance process, the 9-1-1 complex cooperates with polyubiquitinated PCNA and Exo1 nuclease to support switching of the replicative polymerase to the undamaged template (6).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response to hypoxia (1). The HIF1 complex consists of two subunits, HIF-1α and HIF-1β, which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism, and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VHL) E3 ligase complex; ubiquitination and proteasomal degradation follows (3,4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).HIF-1β is also known as AhR nuclear translocator (ARNT) due to its ability to partner with the aryl hydrocarbon receptor (AhR) to form a heterodimeric transcription factor complex (8). Together with AhR, HIF-1β plays an important role in xenobiotics metabolism (8). In addition, a chromosomal translocation leading to a TEL-ARNT fusion protein is associated with acute myeloblastic leukemia (9). Studies also found that ARNT/HIF-1β expression levels decrease significantly in pancreatic islets from patients with type 2 diabetes, suggesting that HIF-1β plays an important role in pancreatic β-cell function (10).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin)

Background: ICOS (Inducible Co-Stimulator, CD278) is a member of the CD28 family that regulates T cell activity and immune responses (1). The ICOS protein contains an extracellular IgV like domain, a transmembrane domain, and an intracellular domain with a YMFM motif (1-2). ICOS is primarily expressed on activated CD4+ and CD8+ T cells (1). Upon binding to its ligand, ICOS potentiates the T cell response to antigen through activation of the PI3K signaling pathway (2). In addition to enhancing T cell activation and proliferation, ICOS plays an important role in the regulation of T follicular helper cells (4). Research studies suggest that ICOS is a potential therapeutic target, and could serve as a prognostic biomarker for neoplastic therapy involving CTLA-4 blockade (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Inhibitor of DNA-binding-2 (Id2) is a member of the Id proteins which belong to the helix-loop-helix (HLH) protein family. The Id protein functions by binding to specific transcription factors and preventing their dimerization and DNA binding (1-3). Id2 interacts with a wide variety of transcription factors including E proteins (5), TCS (4), Pax (6) and the tumor suppressor Rb (1). Id2 has been shown to be important in regulating cellular differentiation, proliferation, development and tumorgenesis (7-9). In tumor cells, increased levels of Id2 functionally inactivate Rb, leading to cellular transformation and cancer (10,11). Id2 is therefore a promising therapeutic target for treatment of cancer (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Inhibitor of DNA-binding/Differentiation (ID) proteins are a family of proteins that function to repress the activity of basic helix-loop-helix (bHLH) transcription factors. There are four known ID proteins in humans (ID1-4), all of which contain a helix-loop-helix domain but lack a basic DNA binding domain. Heterodimerization with bHLH transcription factors therefore functions to sequester bHLH proteins and prevent their binding to DNA (1). ID proteins play important functional roles in development, primarily by inhibiting premature differentiation of stem/progenitor cells (1,2). ID3 plays an important role in immune system development where it has been shown to repress E2A-mediated differentiation of T cells (3). Studies in mouse models have shown that homozygous deletion of ID3 disrupts regulatory T cell differentiation (4) and leads to development of γδ T cell lymphoma (5). Outside of the hematopoietic compartment, ID3 was shown to repress MyoD, implicating ID3 in TGFβ-mediated muscle repair (6). Similarly, research studies have shown that ID3 suppresses p21 in colon cancer cells, a function that is purported to promote the self-renewal capacity of putative cancer-initiating cells (7).

$305
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 IDH1 (D2H1) Rabbit mAb #8137.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP+ respectively, as an electron acceptor (1). IDH1 is the NADP+-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP+ respectively, as an electron acceptor (1). IDH1 is the NADP+-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP+ respectively, as an electron acceptor (1). IDH1 is the NADP+-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: IDH2 is one of three isocitrate dehydrogenases (IDH1-3) that catalyze the oxidative decarboxylation of isocitrate to produce CO2 and α-ketoglutarate (α-KG). These enzymes belong to two distinct subclasses that utilize either NAD or NADP+ as an electron acceptor. IDH2 is an NADP+-dependent isocitrate dehydrogenase expressed primarily in the mitochondria, where it also functions in the TCA cycle (1,2). Mutations in IDH2 or its cytoplasmic counterpart (IDH1) have been reported in glioblastoma multiforme (3), acute myeloid leukemia (4,5), and other malignancies (6). Research studies have shown that gain-of-function mutations in IDH2 can lead to the accumulation and secretion of the oncometabolite R-2-hydroxyglutarate (2HG) in cancer cells (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: IDH2 is one of three isocitrate dehydrogenases (IDH1-3) that catalyze the oxidative decarboxylation of isocitrate to produce CO2 and α-ketoglutarate (α-KG). These enzymes belong to two distinct subclasses that utilize either NAD or NADP+ as an electron acceptor. IDH2 is an NADP+-dependent isocitrate dehydrogenase expressed primarily in the mitochondria, where it also functions in the TCA cycle (1,2). Mutations in IDH2 or its cytoplasmic counterpart (IDH1) have been reported in glioblastoma multiforme (3), acute myeloid leukemia (4,5), and other malignancies (6). Research studies have shown that gain-of-function mutations in IDH2 can lead to the accumulation and secretion of the oncometabolite R-2-hydroxyglutarate (2HG) in cancer cells (6,7).