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Polyclonal Antibody Immunofluorescence Immunocytochemistry Protein Binding

$260
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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: p27 Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. Like its relatives, p57 Kip2 and p21 Waf1/Cip1, the ability to enforce the G1 restriction point is derived from its inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes. Expression levels of p27 are upregulated in quiescent cells and in cells treated with cAMP or other negative cell cycle regulators. Downregulation of p27 can be induced by treatment with interleukin-2 or other mitogens; this involves phosphorylation of p27 and its degradation by the ubiquitin-proteasome pathway (1-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Sodium-dependent neutral amino acid transporter type 2 (ASCT2 or SLC1A5) is a neutral amino acid transporter that regulates the uptake of essential amino acids in conjunction with the SLC7A5 bilateral transporter (1,2). ASCT2 appears to be the major glutamine transporter in hepatoma cells and is thought to provide essential amino acids needed for tumor growth (3). Additional evidence suggests that ASCT2 plays a role in activating mTORC1 signaling and is required to suppress autophagy (4,5). Cell surface ASCT2 serves as a receptor for several mammalian interference retroviruses associated with cases of infectious immunodeficiency; variation in a small region of an extracellular loop (ECL2) may be responsible for species-specific differences in receptor function (6).

$303
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cell death in the fruit fly Drosophila melanogaster is regulated by many of the same stimuli as mammalian cell death (1). The Drosophila genome contains seven caspase genes; three encode initiator caspases, and four encode effector caspases (reviewed in (2)). The Drosophila effector caspase, death caspase-1 (Dcp-1), is a critical executioner of apoptosis. It is involved in the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP). The activation of Dcp-1 requires proteolytic processing of its inactive zymogen into active p22 and p13 fragments (3). Comparison of the in vivo activity between DrICE and Dcp-1 has shown that DrICE is a more effective inducer of apoptosis than Dcp-1, which instead plays a role in determining the rate of cell death (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: p27 Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. Like its relatives, p57 Kip2 and p21 Waf1/Cip1, the ability to enforce the G1 restriction point is derived from its inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes. Expression levels of p27 are upregulated in quiescent cells and in cells treated with cAMP or other negative cell cycle regulators. Downregulation of p27 can be induced by treatment with interleukin-2 or other mitogens; this involves phosphorylation of p27 and its degradation by the ubiquitin-proteasome pathway (1-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: MEP50 (methylosome protein 50) is a component of the methylosome, a protein arginine methyltransferase complex that modifies specific arginine residues found in arginine- and glycine-rich regions of some spliceosomal Sm proteins. MEP50 is important for methylosome activity and may regulate the transfer of Sm proteins to the SMN (survival of motor neurons) complex, an early step in the assembly of U snRNPs. Both the methylosome and the SMN complex are essential for the assembly of spliceosomal snRNPs (1).MEP50 is a WD repeat protein that may provide an interface for multiple protein interactions between methylosome proteins. (1). It binds to JBP1, an arginine protein methyltransferase component of the methylosome. MEP50 has been shown to interact with CTD phosphatase FCP1 (CTDP1), a protein that may link the processes of transcriptional elongation and splicing (2), and with SUZ12, a polycomb group protein involved in transcriptional repression (3). JBP1 and MEP50 have also been reported to interact with the methyl-CpG binding protein complex MBD2/NuRD (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: CD19 is a 95 kDa coreceptor, which amplifies the signaling cascade in B cells (1). On the B cell surface, CD19 associates with CD21, CD81 and Leu-13 to exert its function. The cytoplasmic tail of CD19 has nine conserved tyrosine residues playing critical roles in CD19 mediated function by coupling signaling molecules to the receptor (1). After B cell receptor or CD19 ligation, Tyr531 and Tyr500 of CD19 are progressively phosphorylated. This phosphorylation enables the coupling of PI3 kinase and Src family tyrosine kinase to CD19 and activates the PI3K and Src signaling pathways (2,3). Coligation of B cell receptor and CD19 also promotes Tyr409 phosphorylation in CD19. The phosphorylation at these sites enables its binding to Vav and mediates elevated intracellular calcium response, as well as the JNK pathway (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins having distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with extracellular environment (inside-out signaling) (1,2).The αVβ5 integrin is expressed in various tissues and cell types, including endothelia, epithelia and fibroblasts (4). It plays a role in matrix adhesion to VN, FN, SPARC and bone sialoprotein (5) and functions in the invasion of gliomas and metastatic carcinoma cells (6,7). αVβ5 integrin plays a major role in growth-factor-induced tumor angiogenesis, where cooperative signaling by the αVβ5 integrin and growth factors regulates endothelial cell proliferation and survival (8).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Ca2+ is a key second messenger in many intracellular signaling pathways. Ca2+ signals control many cellular functions ranging from short-term responses such as contraction and secretion to longer-term regulation of cell growth and proliferation (1,2). Stromal interaction molecules (STIMs) function as Ca2+ sensors that detect changes in Ca2+ content in intracellular Ca2+ stores (3). STIM1 is conserved, ubiquitously expressed, and functions as an endoplasmic reticulum (ER) Ca2+ sensor that migrates from the ER Ca2+ store to the plasma membrane where it activates calcium-release-activated calcium (CRAC) channels when the ER Ca2+ store is low (4). STIM1 is a potential tumor suppressor; defects in STIM1 may cause rhabdomyosarcoma and rhabdoid tumors (5). STIM1 can either homodimerize or form heterodimers with STIM2. STIM2 possesses a high sequence identity to STIM1 and can function as an inhibitor of STIM1-mediated plasma membrane store-operated Ca2+ entry (6). However, further investigation is required to elucidate the true physiological function of STIM2.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: In response to genomic stress, the ATR interacting protein (ATRIP) binds and is phosphorylated by the DNA damage-and checkpoint-activated kinase ATR (ataxia-telangiectasia mutated and rad3-related). Both ATR and ATRIP are integral for checkpoint signaling and are critical in the DNA repair response (1-3). Direct interaction between ATRIP and replication protein A (RPA) at RPA-coated, single-stranded DNA results in the recruitment of phosphorylated ATR/ATRIP to stalled replication forks and sites of DNA damage (3). ATR/ATRIP coordinate DNA repair and cell cycle progression in conjunction with key regulatory proteins, such as Rad17 and the 9-1-1 complex (4). ATR associated with ATRIP can also be stimulated by topoisomerase II binding protein (TOPBP1), suggesting that ATRIP may regulate both ATR localization and activity (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Antigen receptors found on the surface of B cells contain a heterodimeric signaling component composed of CD79A and CD79B, also known as Ig α and Ig β, respectively (1,2). Presence of this receptor complex is essential for B-cell development and function (3). Together these two proteins and the associated B cell receptor initiate intracellular signaling following antigen binding (4,5). An immunoreceptor tyrosine-based activation motif (ITAM) found in the CD79A intracellular region appears to be important for its function (6). Antigen binding precedes formation of the CD79A and CD79B heterodimer and subsequent activation of receptor associated kinases (7). Research has shown that CD79A is a marker for B-lineage lymphoblastic leukemia (8). Additionally, investigators have found that mutations in the CD79A (MB1) gene are associated with abnormally low levels of functional B cell receptors in some cases of chronic B cell lymphocytic leukemia (9).

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

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

Background: Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI). RhoGDI affects Rho activity by inhibiting nucleotide exchange and membrane association, regulating activity and localization (Reviewed in 1, 2). The inhibitory and shuttling functions of RhoGDI have been uncoupled using mutant forms of RhoGDI (3). Phosphorylation of GDIs and/or GTPases can modulate their affinity for each other and, therefore, GTPase mediated signaling. PAK1 phosphorylation of RhoGDI at serines 101 and 174 causes release and activation of Rac1, but not RhoA (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Succinate dehydrogenase (SDH), also known as Complex II or succinate:quinone oxidoreductase, is a key component of the citric acid cycle and the electron transport chain (1). Specifically, it is involved in the oxidation of succinate (2). SDH consists of four subunits: SDHA, SDHB, SDHC, and SDHD (3). Research studies have shown that defects in SDHA cause complex II deficiency (2). In addition, investigators have observed reduction of SDHA in the striatum of patients with Huntington’s disease (3), and reduction of SDHB, SDHC, and SDHD in paragangliomas and phenochromocytomas (4,5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CUB domain containing protein 1 (CDCP1, SIMA135) is a putative stem cell marker shown in research studies to be highly expressed in some human cancer cells and in both typical and atypical (cancerous) colons (1). Expression of CDCP1 may be epigenetically regulated, as methylation of promoter CpG sequences results in decreased CDCP1 expression (2). The corresponding CDCP1 gene encodes a glycoprotein that acts as a complex, multidomain transmembrane antigen. CDCP1 has three extracellular CUB domains that may be involved in cell adhesion or extracellular matrix interactions (1,3). Src-family kinases may phosphorylate CDCP1 at five tyrosine residues within its cytoplasmic domain to provide a potential binding site for SH2 domain-containing proteins (3). CDCP1 is a putative hematopoietic stem cell marker (4,5).

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

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

Background: The cohesin complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3) (1,2). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). RAD21 and STAG2 are phosphorylated by Polo-like kinase (PLK) during prophase, which leads to the dissociation of cohesin complexes from the chromosome arms; however, cohesin remains bound to centromeres until anaphase (3,4). RAD21 is cleaved by separin/ESPL1 in anaphase, which leads to dissociation of the remaining cohesin from centromeres, enabling sister chromatids to segregate during mitosis (5). RAD21 is also cleaved by caspase-3 and caspase-7 during apoptosis, resulting in a 64 kDa carboxy-terminal cleavage product that translocates to the cytoplasm and may help to trigger apoptosis (6,7). In addition to mediating cohesion of sister chromatids, the cohesin complex plays important roles in gene regulation and DNA repair, as SMC1 and SMC3 are both phosphorylated by ATM and ATR kinases upon DNA damage (1,2).