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Product listing: Caspase-3 (D3R6Y) Rabbit mAb (IHC Formulated), UniProt ID P42574 #14214 to CBX8 (D2O8C) Rabbit mAb, UniProt ID Q9HC52 #14696

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-5 (Ich-3/ICErelIII/TY) is a member of the caspase family of cysteine proteases that play a key role in the execution of apoptosis and activation of inflammatory cytokines (1-3). Caspase-5 is widely expressed, with highest expression observed in placenta and lung (1). Interferon-γ and LPS regulate expression of caspase-5 (2,4). Members of the caspase-1 subfamily of caspases, which includes caspase-4, -5, and murine caspase-11 and -12, can induce apoptosis when over-expressed and mediate the proteolytic activation of inflammatory cytokines (5). Processing of IL-1β occurs through the activation of an inflammasome complex consisting of caspase-1, caspase-5, Pycard and NALP1 (6). Transcription factor Max, a component of the Myc/Mad/Max network, is cleaved by caspase-5 during Fas-induced apoptosis (7). Several alternative spliced variants of caspase-5 have been identified (8). Frameshift mutations of caspase-5 have been observed in leukemia, lymphoma (9), and colorectal cancers (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis (1-4). Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as (ADP-ribose) polymerase and PARP (1,3). During apoptosis, caspase-7 is activated through proteolytic processing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits (1,3). Similar to caspase-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD (5).

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

Application Methods: Western Blotting

Background: Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis (1-4). Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as (ADP-ribose) polymerase and PARP (1,3). During apoptosis, caspase-7 is activated through proteolytic processing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits (1,3). Similar to caspase-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD (5).

$111
20 µl
$260
200 µl
$630
600 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Apoptosis induced through the CD95 receptor (Fas/APO-1) and tumor necrosis factor receptor 1 (TNFR1) activates caspase-8 and leads to the release of the caspase-8 active fragments, p18 and p10 (1-3). Activated caspase-8 cleaves and activates downstream effector caspases such as caspase-1, -3, -6, and -7. Caspase-3 ultimately elicits the morphological hallmarks of apoptosis, including DNA fragmentation and cell shrinkage.

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

Application Methods: Western Blotting

Background: Apoptosis induced through the CD95 receptor (Fas/APO-1) and tumor necrosis factor receptor 1 (TNFR1) activates caspase-8 and leads to the release of the caspase-8 active fragments, p18 and p10 (1-3). Activated caspase-8 cleaves and activates downstream effector caspases such as caspase-1, -3, -6, and -7. Caspase-3 ultimately elicits the morphological hallmarks of apoptosis, including DNA fragmentation and cell shrinkage.

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

Application Methods: Western Blotting

Background: Caspase-9 (ICE-LAP6, Mch6) is an important member of the cysteine aspartic acid protease (caspase) family (1,2). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with the 47 kDa procaspase-9/Apaf-1. Apaf-1 mediated activation of caspase-9 involves intrinsic proteolytic processing resulting in cleavage at Asp315 and producing a p35 subunit. Another cleavage occurs at Asp330 producing a p37 subunit that can serve to amplify the apoptotic response (3-6). Cleaved caspase-9 further processes other caspase members, including caspase-3 and caspase-7, to initiate a caspase cascade, which leads to apoptosis (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Contactin-associated protein 1 (Caspr) is a membrane protein that is an essential component of the paranodal junctions in the peripheral and central nervous systems (PNS and CNS, respectively). Caspr is part of the Neurexin family of proteins and is also known as Neurexin IV, Paranodin, and Cntnap1. Caspr forms a complex, via its extracellular domain, with contactin at paranodal junctions of the axon (1, 2). Paranodal junctions are specialized junctions in the axon that are formed between the axolemma and the paranodal loops of myelinating glia. Paranodal structures are critical for salutatory conduction in the PNS and CNS. In the absence of Caspr, Caspr knockout mice exhibit mislocalization of other paranodal junction proteins, including contactin and neurofascin (3). Knockout mice also exhibit reduced nerve conduction velocities, as well as behavior defects consistent with abnormal nerve conduction. Therefore, Caspr is a critical component of a protein complex that is likely central to paranodal junction formation and maintenance.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Contactin-associated protein 2 (Caspr2) is a type I transmembrane protein and member of the neurexin superfamily that mediates nervous system cell-cell interactions through the Neurexin IV-Caspr-Paranodin (NCP) complex (1). A multiprotein complex consisting of TAG-1, Caspr2, K+ channel, PSD95 and protein 4.1B mediates the molecular interactions at the juxtaparanodal region of myelinated axons, with homophilic TAG-1 interactions mediating the binding of this complex to glia (2,3).Caspr2 protein localizes to juxtaparanodal regions of myelinated axons where it forms a cis-complex with the immunoglobulin-like cell adhesion molecule TAG-1. Caspr2 also binds to Shaker K+ channels Kv1.1, Kv1.2, and their Kvβ2 subunit. A PDZ domain at the Caspr2 carboxy terminus mediates the Caspr2-K+ channel association. Caspr2 is required for proper K+ channel localization, as Caspr2 deletion causes the redistribution of channels along the internodes (1-3). Furthermore, Caspr2 binds to protein 4.1B and connects the protein complex to the axonal cytoskeleton (4). Mutations in the Caspr2 gene have been linked to focal epilepsy, cortical dysplasia and Gilles de la Tourette syndrome (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CaSR, the extracellular Calcium-Sensing Receptor, is a widely expressed G-protein coupled receptor (GPCR) involved in calcium homeostasis. CaSR operates as a sensor in parathyroid and kidney, and alterations in its activity have been shown to cause thyroid disease in humans (1). Activation of the receptor in response to extracellular calcium or other ligands causes activation of phospholipase C (PLC), release of IP3 and release of calcium from intracellular stores (2). Proinflammatory cytokines IL-1β and TNF-α increase CaSR gene expression in human thyroid and kidney cells through activation of the NF-κB pathway, and this pathway may be involved in hypocalcemia often seen in critically ill patients (3). Elevated calcium concentration and CaSR expression have been linked to proliferation and metastasis of skeletal metastatic prostate cancer cell lines (4). In intestinal epithelial cells, CaSR is involved in regulation of cyclic nucleotide metabolism and the fluid secretion that results in life-threatening fluid loss in response to intestinal pathogens (5). The interaction of CaSR with the actin-binding protein filamin may provide scaffolding for the organization of signaling pathways converging on the cytoskeleton, including CaSR-mediated MAPK pathway activation (6).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Catalase catalyzes the conversion of hydrogen peroxide to water and oxygen (1). Research studies show that overexpression of this antioxidant enzyme increases the ability of pancreatic β-cells to scavenge reactive oxygen species (ROS), thereby protecting pancreatic β-cells from oxidative stress (2). The pancreatic β-cells overexpressing this enzyme are also protected from hydrogen peroxide-mediated lipotoxicity, providing further evidence for the importance of catalase in the pathogenesis of diabetes (3).

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

Application Methods: Western Blotting

Background: Catalase catalyzes the conversion of hydrogen peroxide to water and oxygen (1). Research studies show that overexpression of this antioxidant enzyme increases the ability of pancreatic β-cells to scavenge reactive oxygen species (ROS), thereby protecting pancreatic β-cells from oxidative stress (2). The pancreatic β-cells overexpressing this enzyme are also protected from hydrogen peroxide-mediated lipotoxicity, providing further evidence for the importance of catalase in the pathogenesis of diabetes (3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cathepsin B (D1C7Y) XP® Rabbit mAb #31718.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Cathepsin B (CSTB), part of the papain family of proteases, is a widely expressed lysosomal cysteine endopeptidase (1,2). Cathepsin B is produced from a larger precursor form, pro-cathepsin B, which runs at approximately 44 kDa on SDS-PAGE, and is proteolytically processed and glycosylated to form a mature two-chain protein containing a heavy chain (running at 27 and 24 kDa) and a light chain (5 kDa). High levels of cathepsin B are found in macrophages and osteoclasts, as well as various types of cancer cells, including lung, colon, prostate, breast, and stomach. In addition, expression of cathepsin B has been associated with multiple sclerosis (3), rheumatoid arthritis (4), and pancreatitis (5). While generally localized to lysosomes, in cancer alterations can lead to its secretion (6). Its role in tumor progression is thought to involve promotion of basement membrane degradation, invasion and metastasis (7,8). Expression can correlate with poor prognosis for a variety of forms of cancer (9-13).

$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 Cathepsin B (D1C7Y) XP® Rabbit mAb #31718.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Cathepsin B (CSTB), part of the papain family of proteases, is a widely expressed lysosomal cysteine endopeptidase (1,2). Cathepsin B is produced from a larger precursor form, pro-cathepsin B, which runs at approximately 44 kDa on SDS-PAGE, and is proteolytically processed and glycosylated to form a mature two-chain protein containing a heavy chain (running at 27 and 24 kDa) and a light chain (5 kDa). High levels of cathepsin B are found in macrophages and osteoclasts, as well as various types of cancer cells, including lung, colon, prostate, breast, and stomach. In addition, expression of cathepsin B has been associated with multiple sclerosis (3), rheumatoid arthritis (4), and pancreatitis (5). While generally localized to lysosomes, in cancer alterations can lead to its secretion (6). Its role in tumor progression is thought to involve promotion of basement membrane degradation, invasion and metastasis (7,8). Expression can correlate with poor prognosis for a variety of forms of cancer (9-13).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Cathepsin B (CSTB), part of the papain family of proteases, is a widely expressed lysosomal cysteine endopeptidase (1,2). Cathepsin B is produced from a larger precursor form, pro-cathepsin B, which runs at approximately 44 kDa on SDS-PAGE, and is proteolytically processed and glycosylated to form a mature two-chain protein containing a heavy chain (running at 27 and 24 kDa) and a light chain (5 kDa). High levels of cathepsin B are found in macrophages and osteoclasts, as well as various types of cancer cells, including lung, colon, prostate, breast, and stomach. In addition, expression of cathepsin B has been associated with multiple sclerosis (3), rheumatoid arthritis (4), and pancreatitis (5). While generally localized to lysosomes, in cancer alterations can lead to its secretion (6). Its role in tumor progression is thought to involve promotion of basement membrane degradation, invasion and metastasis (7,8). Expression can correlate with poor prognosis for a variety of forms of cancer (9-13).

$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 Caveolin-1 (D46G3) XP® Rabbit mAb #3267.
APPLICATIONS
REACTIVITY
Bovine, Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

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

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

Background: The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Caveolae ("little caves") are 60-80 nm pits representing specialized plasma membrane domains in many cell types. The principal protein component of caveolae is caveolin, a small integral membrane protein composed of three family members, including the widely expressed caveolin-1 and -2, and the muscle-specific caveolin-3 (1). Caveolin proteins are required for caveolae formation and serve as scaffolding proteins for the recruitment of signaling proteins. Research studies in cavelolin-deficient mice implicate cavelolin proteins in several pathologies, including diabetes, cancer, cardiovascular diseases, atherosclerosis, pulmonary disease, and muscular dystrophies (2).The cavin proteins (cavin-1, -2, -3, and -4 in mammals) are a family of caveolae-associated integral membrane proteins involved in the biogenesis and stability of caveolae. Cavin proteins form homo- or hetero-oligomers whose composition is tissue-specific, which may confer distinct functions of caveolae in various tissues (3). Cavin-1 (PTRF), which is widely expressed, is required for caveolae formation and is thought to play roles in lipid metabolism, adipocyte differentiation, and IGF-1 receptor signaling (4-6). Research studies involving prostate cancer suggest that expression of cavin-1 is related to tumor progression and angiogenesis/lymphangiogenesis (7-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Caveolae ("little caves") are 60-80 nm pits representing specialized plasma membrane domains in many cell types. The principal protein component of caveolae is caveolin, a small integral membrane protein composed of three family members, including the widely expressed caveolin-1 and -2, and the muscle-specific caveolin-3 (1). Caveolin proteins are required for caveolae formation and serve as scaffolding proteins for the recruitment of signaling proteins. Research studies in cavelolin-deficient mice implicate cavelolin proteins in several pathologies, including diabetes, cancer, cardiovascular diseases, atherosclerosis, pulmonary disease, and muscular dystrophies (2).The cavin proteins (cavin-1, -2, -3, and -4 in mammals) are a family of caveolae-associated integral membrane proteins involved in the biogenesis and stability of caveolae. Cavin proteins form homo- or hetero-oligomers whose composition is tissue-specific, which may confer distinct functions of caveolae in various tissues (3). Cavin-1 (PTRF), which is widely expressed, is required for caveolae formation and is thought to play roles in lipid metabolism, adipocyte differentiation, and IGF-1 receptor signaling (4-6). Research studies involving prostate cancer suggest that expression of cavin-1 is related to tumor progression and angiogenesis/lymphangiogenesis (7-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The endocannabinoid system consists of the cannabinoid receptors, CB1 and CB2 receptors, the enzymes that produce and degrade the endogenous cannabinoid ligands (such as FAAH, DAG lipases, and MAG lipase), and the endocannabinoid ligands derived from the metabolism of arachidonic acid, 2-arachidonoylglycerol (2-AG) and anandamide (1-3). CB1 receptor belongs to the superfamily of G protein-coupled receptors (GPCRs) and harbors a large N-terminal extracellular domain, seven transmembrane domains, and a C-terminal intracellular tail. CB1 receptor is coupled to the Gai/o subunit of the G protein which inhibits adenylyl cyclases and regulates calcium and potassium ion channels (4). CB1 receptor is one of the most abundant GPCRs in the central nervous system. It has been show to play critical roles in the wiring of the brain during development (5), in neuronal plasticity (6), analgesia, drug abuse and metabolic homeostasis (7). In addition, CB1 receptor has been shown to interact with other GPCRs, to give rise to novel pharmacological and signaling heteromers with implication in diseases (8,9).

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

Application Methods: Western Blotting

Background: CBARA1/MICU1 is a mitochondrial protein associated to the mitochondrial inner membrane that is comprised of two EF hand helix-loop-helix motifs. CBARA1/MICU1 is involved in mitochondrial calcium entry, metabolic coupling between cytosolic calcium transients, and activation of matrix dehydrogenases (1). Mitochondrial CBARA1/MICU1 is required to preserve normal mitochondrial calcium concentration below the equilibrium level by interacting with the uniporter pore-forming subunit MCU (2). CBARA1/MICU1 is important in pancreatic β-cell mitochondrial calcium uptake and sustained insulin secretion (3).

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

Application Methods: Chromatin IP, Western Blotting

Background: Core-binding factor subunit β (CBFβ) is a non-DNA binding transcription factor subunit that associates with and regulates the DNA binding activity of RUNX1, RUNX2, and RUNX3 (1). CBFβ is ubiquitously expressed and has been implicated in a variety of developmental processes including hematapoiesis, T cell development, chondrogenesis, and bone formation (2-7). In addition, investigators have identified CBFβ as one of the most frequently translocated genes in leukemia (8) and research studies have found it to be required for HIV immune evasion (9,10). CBFβ interacts with the viral protein VIF and triggers assembly of a ubiquitin ligase complex that targets the retroviral inhibitor APOBEC3G for degradation (9,10).

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

Application Methods: Western Blotting

Background: The Casitas B lineage lymphoma (Cbl) proteins (in mammals these are c-Cbl, Cbl-b, and Cbl-c) are a family of single subunit RING finger protein-ubiquitin E3 ligases that contain multiple protein interaction motifs (1). All Cbl proteins have a highly conserved N-terminal tyrosine kinase-binding (TKB) domain that mediates interactions between Cbl proteins and phosphorylated tyrosine residues on Cbl substrates. C-terminal to the RING finger, Cbl proteins have proline-rich domains that mediate interactions with SH3 domain-containing proteins. Phosphorylated tyrosine residues mediate interactions with SH2 domain-containing proteins such as the p85 subunit of PI3K. These protein-protein interaction motifs allow Cbl family proteins to function as adaptor proteins (2). This adaptor function contributes to the E3-dependent activities of Cbl proteins by targeting specific substrates for ubiquitination and degradation. The adaptor function also contributes to non-E3-dependent activities, such as the recruitment of proteins involved in receptor tyrosine kinase internalization, localization of Cbl proteins to specific subcellular compartments, and activation of discrete signaling pathways (1).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: CBP (CREB-binding protein) and p300 are highly conserved and functionally related transcriptional co-activators that associate with transcriptional regulators and signaling molecules, integrating multiple signal transduction pathways with the transcriptional machinery (1,2). CBP/p300 also contain histone acetyltransferase (HAT) activity, allowing them to acetylate histones and other proteins (2). Phosphorylation of p300 at Ser89 by PKC represses its transciptional acitivity, and phosphorylation at the same site by AMPK disrupts the association of p300 with nuclear receptors (3,4). Ser1834 phosphorylation of p300 by Akt disrupts its association with C/EBPβ (5). Growth factors induce phosphorylation of CBP at Ser437, which is required for CBP recruitment to the transcription complex (6). CaM kinase IV phosphorylates CBP at Ser302, which is required for CBP-dependent transcriptional activation in the CNS (7). The role of acetylation of CBP/p300 is of particular interest (2,8). Acetylation of p300 at Lys1499 has been demonstrated to enhance its HAT activity and affect a wide variety of signaling events (9).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: CBP (CREB-binding protein) and p300 are highly conserved and functionally related transcriptional co-activators that associate with transcriptional regulators and signaling molecules, integrating multiple signal transduction pathways with the transcriptional machinery (1,2). CBP/p300 also contain histone acetyltransferase (HAT) activity, allowing them to acetylate histones and other proteins (2). Phosphorylation of p300 at Ser89 by PKC represses its transciptional acitivity, and phosphorylation at the same site by AMPK disrupts the association of p300 with nuclear receptors (3,4). Ser1834 phosphorylation of p300 by Akt disrupts its association with C/EBPβ (5). Growth factors induce phosphorylation of CBP at Ser437, which is required for CBP recruitment to the transcription complex (6). CaM kinase IV phosphorylates CBP at Ser302, which is required for CBP-dependent transcriptional activation in the CNS (7). The role of acetylation of CBP/p300 is of particular interest (2,8). Acetylation of p300 at Lys1499 has been demonstrated to enhance its HAT activity and affect a wide variety of signaling events (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cystathionine beta-synthase (CBS) is a key enzyme involved in sulfur amino acid metabolism because it catalyzes the formation of cystathionine from serine and homocysteine (1,2). The CBS protein contains a heme-binding domain that modulates enzyme activity by sensing redox changes or carbon monoxide binding (1). S-adenosylmethionine binds the carboxyl-terminal CBS domain to allosterically regulate CBS catalytic activity (3,4). In addition to catalyzing cystathionine formation, CBS also catalyzes the generation of hydrogen sulfide, a neuromodulator in the brain, through alternative reactions (5,6). Mutations in the corresponding CBS gene result in homocystinuria, an autosomal recessive disorder characterized by abnormal sulfur metabolism, mental retardation, eye anomalies, and vascular disease (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). CBX4 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7,8). CBX4 itself is a SUMO E3 ligase, and its function influences EMT, DNA damage response, tumor angiogenesis, and self-renewal (9-13).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications: PRC1 and PRC2. PRC1 is a multi-subunit protein complex consisting of a combination of five core protein families: CBX, RING1, PHC, PCGF, and RYPB (5-7). Different combinations of protein family members lead to a diverse array of PRC1 complexes with distinct functions (8). At least two distinct classes of PRC1 complexes have been defined. The first class, known as canonical PRC1, contains RING1, PHC, PCGF and CBX protein subunits, but not RYPB (5-8). This class of PRC1 complexes requires PRC2 and H3K27Me3 for proper recruitment to target genes. CBX proteins mediate recruitment by binding to H3K27Me3. CBX8 in particular is required for repression of many lineage-specific genes during differentiation of hematopoietic stem cells and may play a role in activation of lineage-specific genes during differentiation of embryonic stem cells (9,10). The second class, known as variant PRC1, contains RYPB instead of CBX proteins (5-8). RYBP-containing PRC1 is recruited to chromatin independently of PRC2 and H3K27Me3. These variant PRC1 complexes can function independently of PRC2, or in some cases function upstream to recruit PRC2 complex to target genes.