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Product listing: Chk2 (1C12) Mouse mAb, UniProt ID O96017 #3440 to Cleaved Caspase-3 (Asp175) (5A1E) Rabbit mAb (Biotinylated), UniProt ID P42574 #9654

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

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

Background: Chk2 is the mammalian orthologue of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases (1-3). The amino-terminal domain of Chk2 contains a series of seven serine or threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50, and Thr68) each followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases (4,5). After DNA damage by ionizing radiation (IR), UV irradiation, or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR (5-7). The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 at residues Thr383 and Thr387 in the activation loop of the kinase domain (8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Chk2 is the mammalian orthologue of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases (1-3). The amino-terminal domain of Chk2 contains a series of seven serine or threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50, and Thr68) each followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases (4,5). After DNA damage by ionizing radiation (IR), UV irradiation, or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR (5-7). The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 at residues Thr383 and Thr387 in the activation loop of the kinase domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CHMP2B is a component of the ESCRT III (endosomal sorting required for transport complex III) complex (1, 2). The ESCRT system is composed of the ESCRT-0, -I, -II, and -III complexes, which function sequentially to direct the transport of ubiquitinated transmembrane proteins into the intralumenal vesicles (ILVs), which will eventually mature into multivesicular bodies (MVBs). CHMP2B is a homolog of yeast Vps2, which functions in the ESCRT-II complex to change the initial spiral-structure of snf7 into membrane-sculpting helices for the final pinch off process (3). CHMP2B probably functions similarly in mammalian cells. Research studies show that manipulation of the ESCRT-III complex leads to accumulation of CHMP2B at the plasma membrane and overexpressed CHMP2B polymerizes into a tight helical structure that deforms the shape of associated plasma membrane (4).Research studies have shown that mutation of CHMP2B is associated with frontotemporal dementia, (5, 6). Studies have further shown that the dysfunction of mutant CHMP2B expression may disrupts the normal endo-autophagosome and endo-lysosome pathways and lead to neurodegenerative diseases (6-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Choline kinase (ChoK) catalyzes the phosphorylation of choline, a key step in the biosynthesis of the membrane phospholipid phosphatidylcholine. At least three ChoK isoforms exist in mammalian cells, α-1, α-2, and β. The two α isoforms are transcribed from the same CHKA gene as splice variants, while the β isoform resides on a separate CHKB gene (reviewed in 1).Research studies indicate that ChoKα levels affect signaling through MAPK and Akt pathways (2,3). Investigators have shown that ChoKα plays a role in proliferation and carcinogenesis and is highly expressed/activated in human cancers (4-7). Additional research studies suggest ChoKα may be a potential target for cancer therapy (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye 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 CHOP (L63F7) Mouse mAb #2895.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye 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 CHOP (L63F7) Mouse mAb #2895.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

$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 CHOP (L63F7) Mouse mAb #2895.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

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

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

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

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

Application Methods: Western Blotting

Background: Cofilin is a conserved actin-severing protein required for processes that rely on actin dynamics, including cytokinesis and cell motility (reviewed in 1). Regulation of actin dynamics requires the controlled cycling between the phosphorylated and unphosphorylated forms of cofilin (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at the conserved amino-terminal Ser3 of cofilin (3,4). Slingshot (SSH) phosphatase, for which there have been three mammalian isoforms identified, dephosphorylates cofilin in vivo (5). Chronophin (CIN, PDXP) is a haloacid dehalogenase phosphatase that also dephosphorylates cofilin. Alteration of CIN activity through overexpression of either the wildtype or phosphatase-inactive mutant CIN interferes with actin dynamics, cell morphology and cytokinesis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Iron-sulfur (Fe-S) clusters (ISC) are cofactors for many proteins that display a wide range of biological functions, such as DNA maintenance, transcription, translation, cellular metabolism, electron transport, and oxidative phosphorylation (1). While structurally simple, the synthesis and insertion of ISC into Fe-S proteins are complex processes that involve many different proteins. The cytosolic iron-sulfur assembly component 1 (CIAO1) protein is a key component of the cytosolic ISC assembly machinery that incorporates ISC into cytoplasmic and nuclear Fe-S proteins in eukaryotic cells (1,2). CIAO1, along with MMS19, XPD, FAM96B, and ANT2, comprise a complex that localizes to the mitotic spindle during mitosis, which suggests a role in chromosome segregation (3-6). The CIAO1 protein interacts with Wilms' tumor suppressor protein (WT1) and may affect its transactivation activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Iron-sulfur (Fe-S) clusters (ISC) are cofactors for many proteins that display a wide range of biological functions, such as DNA maintenance, transcription, translation, cellular metabolism, electron transport, and oxidative phosphorylation (1). While structurally simple, the synthesis and insertion of ISC into Fe-S proteins are complex processes that involve many different proteins. The cytosolic iron-sulfur assembly component 1 (CIAO1) protein is a key component of the cytosolic ISC assembly machinery that incorporates ISC into cytoplasmic and nuclear Fe-S proteins in eukaryotic cells (1,2). CIAO1, along with MMS19, XPD, FAM96B, and ANT2, comprise a complex that localizes to the mitotic spindle during mitosis, which suggests a role in chromosome segregation (3-6). The CIAO1 protein interacts with Wilms' tumor suppressor protein (WT1) and may affect its transactivation activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CIN85 was independently identified as Cbl-interacting protein of 85 kDa (1), Ruk (regulator of ubiquitous kinase) (2), SETA (SH3 domain-containing gene expressed in tumorigenic astrocytes) (3), and SH3KBP1 (SH3 domain kinase binding protein 1) (4). The genes encoding these proteins were isolated from either human (CIN85), rat (Ruk and SETA), or mouse (SH3KBP1) sources and share between 92% and 97% sequence identity, suggesting that they represent homologues of one gene. Differential promoter usage and alternative splicing is thought to occur in a tissue specific and developmentally regulated manner to generate a complex expression pattern of various transcripts and encoded protein isoforms (5). The main isoform in humans, CIN85, contains three N-terminal SH3 domains, a proline-rich region harboring several P-X-X-P motifs that provide recognition sites for SH3 domain-containing proteins, a PEST sequence implicated in CIN85 degradation, and a C-terminal coiled-coil region for oligomerization (1,2,5,6). The other molecular variants of CIN85 are shorter, N-terminally truncated proteins lacking one, two, or all three of the SH3 domains (1,5,6-8). Proteomic screens suggest that CIN85 is phosphorylated at multiple sites and the role of phosphorylation of some of these sites in regulation of intra- and intermolecular interactions of CIN85 cannot be excluded. CIN85 belongs to the CD2AP/CMS family of adaptor proteins and has been shown to interact with signaling molecules such as c-Cbl, Cbl-b, BLNK, p85/PI3K, GRB2, p130 Cas, and endophilins to coordinate the activity of multiple signaling cascades. Indeed, a growing body of evidence suggests that CIN85 is required for the regulation of a variety of cellular processes including vesicle-mediated transport (9-12), signal transduction (13,14), and cytoskeleton remodelling (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein phosphatase 2A (PP2A) is a trimeric protein phosphatase and tumor suppressor that regulates the phosphorylation status of a wide variety of phosphoproteins. PP2A targets include many that play a role in the maintenance and progression of cancer (1). The cancerous inhibitor of protein phosphatase 2A (CIP2A) is a single pass membrane protein that binds the PP2A catalytic subunit to inhibit PP2A phosphatase activity (2). CIP2A is normally expressed at low levels in normal cells and tissues, but is elevated in human malignancies where it is thought to be oncogenic. Research studies demonstrate aberrant CIP2A expression in multiple tumor types, including those derived from the head and neck, liver, colon, lung, osteosarcoma, pancreatic, breast, and myeloid cancers (reviewed in 3). This evidence suggests that CIP2A interacts with many proteins that may play a role in cancer maintenance and progression (3). Additional studies indicate that CIP2A inhibits PP2A-mediated dephosphorylation of the proto-oncogene Myc at Ser64, which stabilizes and prevents proteolytic degradation of the Myc transcription factor (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cold-induced RNA-binding protein (CIRBP) is a 172-residue, multifunctional sensor protein that was first isolated as a protein induced in mouse fibroblasts cultured at 32ºC (1). Conversely, CIRBP expression decreases in cells or tissues subjected to increased temperature (2). The CIRBP protein is composed of an amino-terminal RNA-binding domain and a carboxyl-terminal, glycine-rich domain (1). Stressful stimuli, such as hypoxia, heat shock, osmotic shock, or oxidative conditions, lead to translocation of CIRBP from the nucleus to cytoplasmic stress granules through a mechanism involving CIRBP methylation-dependent nuclear export (3). CIRBP plays a role in regulating apoptosis and preserving the stemness of neural stem cells at moderately low temperatures (4). Research studies demonstrate that CIRBP contributes to the regulation of circadian rhythm through post-translational modulation of CLOCK expression (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CDGSH iron-sulfur domain-containing protein 1 (CISD1), also known as mitochondrial outer membrane iron-sulfur (2Fe-2S) protein (mitoNEET) was first identified as the target for the drug pioglitazone, used to treat diabetes (1-3). CISD1/mitoNEET regulates both mitochondrial iron transport into the matrix and mitochondrial respiratory capacity. It has also been shown to affect the dynamics of cellular and whole-body lipid homeostasis (2,4). Furthermore, research studies have shown that CISD1/mitoNEET is overexpressed in human epithelial breast cancer cells and it has been considered a potential chemotherapeutic target (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway (1-3). The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway (1-3). The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses.

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Citrate synthase (CS) is a mitochondrial enzyme that catalyzes the first and rate-limiting reaction of the citric acid cycle (1,2). The enzyme is responsible for the conversion of oxaloacetate and acetyl-CoA to citrate and CoA (1,2). Research studies show that CS knockdown HeLa cells are more malignant than vector-transfected cells from an in vivo xenograft model, which suggests a direct link between the Warburg Effect and tumor growth (2). Intervertebral disc degeneration, a growing health problem, has been linked to changes in citrate synthase activity (3). 

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

Application Methods: Western Blotting

Background: Microtubules (MTs) are polarized cellular filaments composed of α/β tubulin heterodimers. The slower growing (minus) microtubule ends are located at MT organizing centers (MTOCs), with the faster growing (plus) ends extending to the cell periphery. The regulation of MT dynamics is an important part of several biological processes, including cell division, migration, adhesion, membrane trafficking, and polarity (1).Human cytoplasmic linker-associate proteins 1 and 2 (CLASP1 and CLASP2) are evolutionarily conserved proteins that localize to the plus ends of interphase microtubules. During mitosis, CLASP 1 and CLASP2 localize to the centrosomes and kinetochores (KT) where they regulate mitotic spindle positioning to ensure proper chromosome alignment (2,3). Research studies indicate that phosphorylation of the carboxy terminus of CLASP2 during mitosis by CDK1 and PLK1 is required for efficient mitotic MT-KT attachment (4). Phosphorylation of CLASP2 at Ser1013 is a critical step that primes CLASP2 for further phosphorylation by PLK1 (4). The additional phosphorylation of CLASP2 at Ser533 and Ser537 by GSK3-3β controls the distribution of CLASP2 on MTs by inhibiting CLASP2 interaction with the Rac1/cdc42 effector protein IQGAP1 (5).

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

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

Background: Clathrin-coated vesicles provide for the intracellular transport of cargo proteins following endocytosis and during multiple vesicle trafficking pathways. Vesicles form at specialized areas of the cell membrane where clathrin and associated proteins form clathrin-coated pits. Invagination of these cell membrane-associated pits internalizes proteins and forms an intracellular clathrin-coated vesicle (1,2). Clathrin is the most abundant protein in these vesicles and is present as a basic assembly unit called a triskelion. Each clathrin triskelion is composed of three clathrin heavy chains and three clathrin light chains. Clathrin heavy chain proteins are composed of several functional domains, including a carboxy-terminal region that permits interaction with other heavy chain proteins within a triskelion, and a globular amino-terminal region that associates with other vesicle proteins (2). Adaptor proteins, such as AP2, epsin and EPS15, are responsible for the recruitment of vesicle proteins to sites of pit formation and the assembly of the clathrin-coated vesicle. Following vesicle invagination, the GTPase dynamin constricts the neck of the nascent vesicle to complete formation of the free, cytosolic vesicle (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Human

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

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin)

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Chloride channel 3 (CLCN3) is a voltage-gated chloride channel (CIC) family protein that mediates H+/Cl- exchange across cell membranes. This 818 amino acid, multi-pass membrane protein is highly expressed in the brain and is especially abundant in the olfactory bulb, hippocampus, and cerebellum (1). CLCN3 protein localizes to endosomal compartments and synaptic vesicles where it contributes to vesicle acidification and proper synaptic vesicle neurotransmitter loading for GABAergic synaptic transmission (2,3). CAMKII-mediated phosphorylation of CLCN3 regulates chloride channel activity by regulating cell surface targeting of the CLCN3 chloride channel (4). Research studies show abnormally high CLCN3 expression at the cell surface of human glioma cells, and that CAMKII-dependent regulation of these channels contributes to glioma invasion (5).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).

$327
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cleaved Caspase-3 (Asp175) (5A1E) Rabbit mAb #9664.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).