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Product listing: CEA/CD66e (CB30) Mouse mAb, UniProt ID P06731 #2383 to Bax Antibody, UniProt ID Q07812 #2774

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Carcinoembryonic antigen (CEA), also known as CD66e or CEACAM5, is a 180-200 kDa cell surface glycoprotein whose expression is elevated in intestinal carcinomas and other tumors. CEA mediates cell adhesion, though little more is known about its biological activity. Expression of CEA is correlated with tumerogenicity (1), and it has been shown to play a role in cell migration, adhesion and invasion in culture cells, as well as in metastasis in vivo (2).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse

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

Background: LIM-containing lipoma-preferred partner (LPP) belongs to the zyxin family, members of which include LIMD1, ajuba, trip6 and zyxin. Three LIM domains at the carboxy-terminus characterize this family of proteins. Zyxin family members associate with the actin cytoskeleton and are components of both the cell-cell junction adhesive complex and the integrin-mediated adhesive complex (1). They shuttle in and out of the nucleus where they may function in transcriptional activation (1).LPP binding partners at cell-cell contacts include the actin regulator α-actinin (2) and the human tumor suppressor scrib which regulates cell migration and polarity (3).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The ADAM (A Disintegrin and A Metalloprotease) family of multidomain membrane proteins influences cell signaling and adhesion by shedding cell surface proteins such as cytokines and growth factors, by influencing cell adhesion to the extracellular matrix (ECM), and by directly remodeling the ECM. Conserved domains in ADAM family members include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).The prodomain is thought to aid in protein folding. Disintegrin and cysteine-rich domains mediate adhesion, at least in part, through binding to integrins. Phosphorylation of the cytoplasmic tail as well as its interaction with other signaling proteins may influence intra- and extracellular signaling (1). ADAM9 is widely distributed and has been shown to affect migration in skin keratinocytes (3,4). Research studies have shown that ADAM9 is overexpressed in prostate cancer (5), pancreatic cancer (6), gastric cancer (7), and has been linked to invasion and metastasis in small cell lung cancer (8). Research has also shown that an alternatively spliced short (50 kDa) form of ADAM9 containing protease activity is involved in tumor cell invasion (9).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calpain is a calcium-dependent thiol proteinase that is functionally active as a heterodimer composed of a small regulatory subunit and one of at least two large catalytic subunits (calpain 1 or calpain 2). In vitro, calpain 1 (mu-calpain) requires micromolar levels of calcium, while calpain 2 (M-calpain) requires millimolar levels of calcium for activation. The regulation of calpain in vivo is the subject of many current studies, which suggest that proteolytic activity is regulated post-transcriptionally by mechanisms such as calcium requirements, subcellular localization of the heterodimer, phosphorylation via the EGFR-Erk signaling cascade, endogenous inhibitors (calpastatin) and autoproteolytic cleavage (1). Calpastatin negatively regulates autoproteolytic cleavage of calpain 1 between Gly27 and Leu28 (2). Calpain influences cell migration by modifying rather than degrading its substrates responsible for cell adhesion and cytoskeletal arrangement. Control of calpain activity has caught the attention of drug development since limiting its activity could mute invasiveness of tumors or chronic inflammation (1).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calpain is a calcium-dependent thiol proteinase that is functionally active as a heterodimer composed of a small regulatory subunit and one of at least two large catalytic subunits (calpain 1 or calpain 2). In vitro, calpain 1 (mu-calpain) requires micromolar levels of calcium, while calpain 2 (M-calpain) requires millimolar levels of calcium for activation. The regulation of calpain in vivo is the subject of many current studies, which suggest that proteolytic activity is regulated post-transcriptionally by mechanisms such as calcium requirements, subcellular localization of the heterodimer, phosphorylation via the EGFR-Erk signaling cascade, endogenous inhibitors (calpastatin) and autoproteolytic cleavage (1). Calpastatin negatively regulates autoproteolytic cleavage of calpain 1 between Gly27 and Leu28 (2). Calpain influences cell migration by modifying rather than degrading its substrates responsible for cell adhesion and cytoskeletal arrangement. Control of calpain activity has caught the attention of drug development since limiting its activity could mute invasiveness of tumors or chronic inflammation (1).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Cathepsin D is a ubiquitously expressed lysosomal aspartyl protease involved in the normal degradation of proteins (1). It is synthesized as an inactive 43 kDa preprocathepsin D that is cleaved and glycosylated to form a 46 kDa procathepsin D and then further cleaved to produce 28 kDa and 15 kDa subunits (heavy and light chains, respectively) (2). Cathepsin D may also be secreted into the cytosol during apoptosis and contribute to cleavage of substrates implicated in the apoptotic pathway (3). Numerous studies have suggested that cathepsin D plays a role in neuronal degradation and malignant transformation, particularily in breast cancer (4-9).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: G-protein coupled receptor (GPCR) kinase interacting proteins 1 and 2 (GIT-1 and GIT-2) are highly conserved, ubiquitous scaffold proteins involved in localized signaling to help regulate focal contact assembly and cytoskeletal dynamics. GIT proteins contain multiple interaction domains that allow interaction with small GTPases (including ARF, Rac and cdc42), kinases (such as PAK and MEK), the Rho family GEF PIX, and the focal adhesion protein paxillin (reviewed in 1). GIT-1 is localized to focal adhesions, cytoplasmic complexes and membrane protrusions, and regulates cell protrusion formation and cell migration (2). GIT-1 has also been implicated in neuronal functions including synapse formation (3) and the pathology of Huntington disease (4). Huntington disease is a genetic neurodegenerative condition involving a mutation in the huntington gene. The huntington gene product (htt) is ubiquitinated and degraded in human Huntington disease brains (5). Htt interacts directly with GIT-1 causing enhanced htt proteolysis, indicating that GIT-1 distribution and function may contribute to Huntington disease pathology (4).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

Background: Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-FAK (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: βIG-H3 (TGFBI/RGD-CAP/Kerato-epithelin) is a 683-amino acid secretory protein induced by TGF-β that plays a role in cell adhesion, differentiation, and apoptosis (1-4). βIG-H3 contains an internal cysteine-rich EMI domain followed by four fasciclin-1 domains and a carboxy terminal RGD domain (1,2). It contributes to cell adhesion through interactions with integrins as well as a number of extracellular matrix (ECM) proteins including collagen, fibronectin, and laminin (5-7). ECM βIG-H3 is found in a wide variety of tissues (8-12). Mutations in the βIG-H3 gene as well as elevated protein levels are most notably associated with corneal dystrophies (13).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

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

Background: Also known as plakoglobin, γ-catenin is a member of the Armadillo family of signaling molecules, which includes β-catenin and the Drosophila protein armadillo (1). This family of proteins is involved in Wnt signaling, which is important in embryonic development and in tumorigenesis (2-3). Although the two vertebrate proteins β- and γ-catenin display sequence homology, γ-catenin likely plays a role distinct from that of β-catenin (1, 4-6). γ-catenin localizes to desmosomes and adherens junctions, both sites of intercellular adhesion, and interacts with the cytoplasmic domains of classical and desmosomal cadherins. Interaction of γ- or β-catenin with α-catenin, desmoplakin and other junction proteins provides a link between intercellular junctions and the actin and intermediate filament cytoskeleton. Maintenance and/or modification of this link is vital for control of cell adhesion and migration (1). γ-catenin is modified by phosphorylation, affecting both adhesion and β-catenin dependent transcription (7), and by and O-glycosylation, affecting adhesion (8). Recent evidence suggests that γ-catenin regulates desmosomal adhesion in response to growth factor stimulation (9).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Alix, a phylogenetically conserved cytosolic scaffold protein, contains an N-terminal Bro1 domain, a coiled-coil region and a C-terminal proline-rich domain (1,2). Originally identified as an ALG-2 (apoptosis-linked gene 2)-interacting protein involved in programmed cell death (3,4), Alix also regulates many other cellular processes, such as endocytic membrane trafficking and cell adhesion through interactions with ESCRT (endosomal sorting complex required for transport) proteins, endophilins, and CIN85 (Cbl-interacting protein of 85 kDa) (5,6).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The sequence-specific transcription factor activator protein 2α (AP-2α) is required for normal growth and morphogenesis during mammalian development (1,2). Decreased or loss of AP-2α expression has been observed in many different types of human cancers including breast cancer (3,4), ovarian cancer (5), melanoma (6) and prostate cancer (7). These findings suggest that AP-2α expression plays a crucial role in tumorigenicity. Studies have also shown that p53 overexpression in human breast carcinoma cells induces the level of AP-2α expression. Furthermore, p53 binds to the cis-element in the AP-2α promoter, suggesting that AP-2α is a target of p53. AP-2α may mediate the effect of p53 to inhibit cell proliferation (8).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: DRAK2 (DAP kinase related apoptosis inducing protein kinase 2) is a member of the novel DAP (death associated protein) pro-apoptotic kinase family (1). Overexpression of DRAK2 in NIH/3T3 cells induces morphological changes associated with apoptosis, which are likely to occur in a p53-dependent manner (1,2). DRAK2 is preferentially expressed in lymphoid tissues and regulates the TCR activation threshold during thymocyte selection (3). Indeed, T cells from DRAK2(-/-) mice exhibit enhanced sensitivity to T cell receptor-mediated stimulation and have a reduced requirement for co-stimulation (4).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Smac/Diablo is a 21 kDa mammalian mitochondrial protein that functions as a regulatory component during apoptosis (1,2). Upon mitochondrial stress, Smac/Diablo is released from mitochondria and competes with caspases for binding of IAPs (inhibitor of apoptosis proteins) (1,2). The interaction of Smac/Diablo with IAPs relieves the inhibitory effect of the IAPs on caspases (3,4). This interaction involves mainly the amino-terminal residues of Smac/Diablo with the BIR3 region of XIAP, supplemented with several other hydrophobic interactions between the helical structures of Smac/Diablo and other areas of BIR3 (5,6).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL), also referred to as Apo2 ligand, first identified based on its sequence homology to TNF and Fas/Apo ligand is a member of the TNF family of cytokines and either exists as a type II membrane or soluble protein (1,2). TRAIL induces apoptosis in a variety of transformed cell lines and plays a role in anti-tumor and anti-viral immune surveillance (3). TRAIL signals via binding with death receptors DR4 (TRAIL-R1) (4) and DR5 (TRAIL-R2) (5-8) which can trigger apoptosis as well as NF-κB activation (7,9). Death domains on these receptors leads to the recruitment of a death-induced signaling complex (DISC) leading to caspase-8 and subsequent caspase-3 activation. In addition, TRAIL binds with decoy receptors DcR1 (TRAIL-R3) (10-13) and DcR2 (TRAIL-R4, TRUNDD) (14-15) which lack the functional cytoplasmic death domain antagonizing TRAIL-induced apoptosis. Osteoprotegerin (OPG) has also been identified as receptor capable of inhibiting TRAIL-induced apoptosis (16). The selectivity of soluble TRAIL at triggering apoptosis in transformed cells as compared to normal cells has led to its investigation as a potential cancer therapeutic (17-18).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Fodrin (also named nonerythroid spectrin) is a universally expressed membrane-associated cytoskeletal protein consisting of alpha- and beta-subunits (1). This protein is important for maintaining normal membrane structure and supporting cell surface protein function (1). Alpha-fodrin is one of the primary targets cleaved by caspases during apoptosis. The full length 240 kDa protein can be cleaved at several sites within its sequence by activated caspases to yield amino-terminal 150 kDa, carboxy-terminal 120 kDa and 35 kDa major products (2-5). Cleavage of alpha-fodrin leads to membrane malfunction and cell shrinkage.

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The sequence-specific transcription factor activator protein 2α (AP-2α) is required for normal growth and morphogenesis during mammalian development (1,2). Decreased or loss of AP-2α expression has been observed in many different types of human cancers including breast cancer (3,4), ovarian cancer (5), melanoma (6) and prostate cancer (7). These findings suggest that AP-2α expression plays a crucial role in tumorigenicity. Studies have also shown that p53 overexpression in human breast carcinoma cells induces the level of AP-2α expression. Furthermore, p53 binds to the cis-element in the AP-2α promoter, suggesting that AP-2α is a target of p53. AP-2α may mediate the effect of p53 to inhibit cell proliferation (8).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The sequence-specific transcription factor activator protein 2β (AP-2β) is required for normal kidney development (1). AP-2β knockout mice die 1-2 days after birth due to polycystic kidney disease (1). Massive apoptosis occured during kidney deveopment at the end of embryogenesis in these mice (1). Overexpressed AP-2β has been to found to suppress c-myc-induced apoptosis, indicating a role of this transcription factor in cell survival (1). In addition, overexpression of AP-2β is shown to be related to impaired insulin signaling in adipocytes, and is therefore proposed to be a candidate gene that may relate to obesity (2).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Activator protein 2γ (AP-2γ) is a member of the developmentally-regulated transcription factor activator protein 2 family (1). Overexpression of p53 in human breast cancer cells increases AP-2γ mRNA and protein (2). In addition, p53 binds to the AP-2γ promoter, suggesting that AP-2γ is a target of p53. AP-2γ therefore may contribute to p53-mediated growth inhibition (2). Studies also found that AP-2γ increases p21 mRNA and protein levels and induces cell-cycle arrest in G1 phase (3). Overexpression of AP-2γ inhibits the growth of human breast cancer cells (3). Taken together, these findings suggest that AP-2γ functions as a tumor suppressor (3).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The Bcl-2 family regulates apoptosis in response to a wide range of stimuli through control of mitochondrial cytochrome c release and caspase activation (1-3). Cytosolic Apaf-1 forms a complex with caspase-9 in the presence of cytochrome c and dATP, ultimately leading to caspase-9 activation and subsequent activation of caspase-3. A large number of proteins have been found to interact with Bcl-2 and other family members that have been shown to help regulate apoptosis. Aven was identified in a yeast two-hybrid screen as a bcl-xL interacting protein (4). It also interacts with other anti-apoptotic family members, including Bcl-2, but fails to interact with pro-apopotic proteins Bax and Bak. Aven inhibits apoptosis and enhances anti-apopotic activity of Bcl-xL. It interferes with association with Apaf-1 and activation of caspase-9. Aven overexpression is associated with poor prognosis in acute lymphoblastic leukemia (5,6).

$255
10 western blots
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Bax is a key component for cellular induced apoptosis through mitochondrial stress (1). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (2). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (3,4).