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Product listing: MTA1 (D40D1) XP® Rabbit mAb, UniProt ID Q13330 #5647 to PAK2 (C17A10) Rabbit mAb, UniProt ID Q13177 #2615

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: MTA1 (metastasis associated gene 1) was identified in a differential screening of a cDNA library of metastatic and nonmetastatic adenocarcinoma cell lines (1), and was subsequently found to be an integral member of the nucleosome remodeling and deacetylation (NuRD) complex (2,3). MTA1 expression is upregulated under hypoxic conditions and found to enhance angiogenesis through stabilization of HIF-1α (4,5). MTA1 is overexpressed in a wide range of human cancers, and its expression is associated with malignancy and tumor progression (6). MTA1 is an essential downstream effector of c-Myc transformation (7). Recently, MTA1 was demonstrated to play a role in DNA damage response (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fanconi anemia (FA) is an autosomal recessive genetic disorder that results in chromosomal breakage, bone marrow failure, hypersensitivity to DNA cross-linking agents (such as mitomycin C), and a predisposition to cancer (1). The ubiquitously expressed FA complementation group A protein (FANCA, FAA) is a component of the FA nuclear complex that also contains FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, and FANCM. In response to DNA damage, the FA nuclear complex induces mono-ubiquitination of FANCD2 and FANCI (2). FANCJ/BRIP1, FANCD1/BRCA2 and FANCN/PALB2 are then recruited to sites of DNA damage along with other DNA repair proteins. FA signaling is important in maintenance of chromosome stability and control of mitosis (3).DNA-damage-dependent localization and stability of FANCA protein regulates FA complex function and localization. Interaction between FANCA protein and the Hsp90 chaperone protein regulates FANCA protein stability and turnover, and may play a role in controlling the FA DNA damage pathway (4). Mutations in the corresponding FANCA gene are responsible for the majority of cases of Fanconi anemia (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Glucocorticoid hormones control cellular proliferation, inflammation, and metabolism through their association with the glucocorticoid receptor (GR)/NR3C1, a member of the nuclear hormone receptor superfamily of transcription factors (1). GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which also contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. On hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with specific DNA sequences termed glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes (2). It was demonstrated that GR-mediated transcriptional activation is modulated by phosphorylation (3-5). Although GR can be basally phosphorylated in the absence of hormone, it becomes hyperphosphorylated upon binding receptor agonists. It has been suggested that hormone-dependent phosphorylation of GR may determine target promoter specificity, cofactor interaction, strength and duration of receptor signaling, receptor stability, and receptor subcellular localization (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Friend leukemia integration 1 (FLI1) transcription factor is an ETS domain-containing transcription factor that plays an important and highly conserved role in vertebrate development, particularly hematopoiesis, where it functions to activate transcription of genes that promote erythroblast proliferation (1-4). In mice, the Fli1 locus is a common retroviral insertion site for the Friend murine leukemia virus (F-MuLV), such that a majority of F-MuLV-induced erythroleukemias are associated with aberrant Fli1 expression (5). Notably in humans, aberrant FLI1 expression has also been linked to poor prognosis in acute myeloid leukemia (6). Also in humans, a t(11;22)(q24;q12) chromosomal translocation has been described that generates a chimeric protein (EWS/FLI1) comprised of the amino-terminal transactivation domain of Ewing's sarcoma breakpoint region 1 (EWS) and the carboxy-terminal ETS domain of FLI1 (7). The EWS/FLI1 fusion protein functions as a transcriptional activator that is reportedly responsible for >85% of the known cases of pediatric Ewing’s sarcoma, an aggressive bone and soft tissue tumor (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Translation initiation requires a set of factors to facilitate the association of the 40S ribosomal subunit with mRNA. The eIF4F complex, consisting of eIF4E, eIF4A, and eIF4G, binds to the 5' cap structure of mRNA. eIF4F and eIF4B unwind the secondary structure of mRNA at its 5' untranslated region. The 40S ribosomal subunit, along with some initiation factors including eIF3, then binds to the 5' mRNA cap and searches along the mRNA for the initiation codon. eIF3 is a large translation initiation complex with 10 to 13 different subunits. eIF3A, eIF3B, eIF3C, eIF3E, eIF3F, and eIF3H are the core subunits critical for the function of this complex. eIF3 physically interacts with eIF4G, which may be responsible for the association of the 40S ribosomal subunit with mRNA (1). eIF3 also stabilizes the binding of Met-tRNAf.eIF2.GTP to the 40S ribosomal subunit and helps keep the integrity of the resulting complex upon addition of the 60S ribosomal subunit (2). Studies have shown that mTOR interacts with eIF3 directly (3,4). When cells are stimulated by hormones or mitogenic signals, mTOR binds to the eIF3 complex and phosphorylates S6K1 (3). This process results in the dissociation of S6K1 from eIF3 and S6K1 activation. The activated S6K1 then phosphorylates its downstream targets including ribosomal protein S6 and eIF4B, resulting in stimulation of translation. Further findings demonstrated that activated mTOR signaling induces the association of eIF3 with eIF4G upon stimulation with insulin (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ron is a member of the Met protooncogene family of receptor tyrosine kinases, which also includes Stk, c-Met, and c-Sea. The functional Ron is a heterodimer composed of a 40 kDa α chain and a 150 kDa β chain. Ron is initially synthesized in the cells as a single-chain, pro-Ron precursor that is cleaved into the two active chains. The α chain is completely extracellular, whereas the β chain traverses the cell membrane and contains the intracellular tyrosine kinase and regulatory elements (1,2). Ron mediates multiple signaling cascades that involve cell motility, adhesion, proliferation, and apoptosis. The signaling pathways activated downstream of Ron include the ras/mitogen-activated protein kinase (MAPK), phosphatidyl inositol-3 kinase (PI3K)/Akt, and focal adhesion kinase (FAK) pathways. Ron activation can also significantly increase c-Src activity, a signaling intermediate involved in cell cycle progression, motility, angiogenesis and survival (3,4). The function of Ron has been shown to be important for embryological development as well as implicated in the progression and metastasis of tumors (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Signal Transducing Adaptor Molecule 1 (STAM1) is a ubiquitously expressed adaptor protein containing an SH3 domain and an ITAM motif. Initial research studies demonstrated that STAM1 undergoes tyrosine phosphorylation following treatment with numerous cytokines and growth factors (1). Subsequent research studies identified STAM1 as a component of the ESCRT-0 complex, which mediates the endocytic sorting of ubiquitinated membrane proteins to the lysosomal compartment for degradation (2). STAM1 harbors a tandemly-oriented VHS (Vps27/Hrs/STAM) domain and UIM (ubiquitin-interacting motif) that facilitates STAM1 binding to ubiquitinated cargo proteins within the endosomal compartment (3,4). Gene targeting studies have revealed that STAM1 and STAM2 cooperate to promote thymic T-cell development and survival (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The DYRK family includes several dual-specificity tyrosine-phosphorylated and regulated kinases capable of phosphorylating proteins at both Tyr and Ser/Thr residues (1). The DYRK family was identified based on homology to the yeast Yak1 (2) and the Drosophila minibrain (mnb) kinases (3). Seven mammalian isoforms have been discovered, including DYRK1A, DYRK1B, DYRK1C, DYRK2, DYRK3, DYRK4, and DYRK4B. Differences in substrate specificity, expression, and subcellular localization are seen across the DYRK family (4,5). All DYRK proteins have a Tyr-X-Tyr motif in the catalytic domain activation loop; phosphorylation of the second Tyr residue (e.g. Tyr312 of DYRK1A) is necessary for kinase activity. DYRKs typically autophosphorylate the Tyr residue within their activation loop, but phosphorylate substrates at Ser and Thr residues (1,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Wolfram syndrome protein (WFS1) is an 890 amino acid protein that contains a cytoplasmic N-terminal domain, followed by nine-transmembrane domains and a luminal C-terminal domain. WFS1 is predominantly localized to the endoplasmic reticulum (ER) (1) and its expression is induced in response to ER stress, partially through transcriptional activation (2,3). Research studies have shown that mutations in the WFS1 gene lead to Wolfram syndrome, an autosomal recessive neurodegenerative disorder defined by young-onset, non-immune, insulin-dependent diabetes mellitus and progressive optic atrophy (4).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The NDK/NME/NM23 kinase family (encoded by the NME gene family) consists of at least eight distinct proteins that exhibit different cellular localization (1). Members of this group inhibit metastasis in a variety of tumor cell types (2). All NDK/NME/NM23 proteins possess nucleoside diphosphatase kinase (NDK) activity and catalyze the phosphorylation of nucleoside diphosphate to the corresponding nucleoside triphosphate to regulate a diverse array of cellular events (3). At least four classes of NDK biochemical activities have been described, including protein-protein interactions (4-6), regulation of GTP-binding protein function (7-9), DNA-associated activities (10,11), and histidine-dependent protein phosphotransferase activity (12). NDK/NME proteins participate in the regulation of a broad spectrum of cellular responses, including development, differentiation, proliferation, endocytosis, and apoptosis (13). Because of its role in metastasis suppression and oncogenesis, NDKA (NME1/NM23-H1) has been widely studied (14). NDKA (NM23-H1) and NDKB (NM23-H2) are encoded by adjacent NME1 and NME2 genes and share 90% sequence identity. Two serine residues (Ser122 and Ser144) on NDKA/NM23-H1 can be phosphorylated by AMPKα1, but only phosphorylation at Ser122 determines whether NDKA channels ATP to AMPKα1. This regulates AMPKα1 activity towards ACC1, an important regulator of fatty acid metabolism (15). Mutation of NDKB/NM23-H2 at Ser122 (S122P) in melanoma cells results in altered phosphoryl transfer activity (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Ewing sarcoma (EWS) protein is a member of the multifunctional FET (FUS, EWS, and TAF15) family of proteins (1,2). These proteins are RNA and DNA binding proteins that are thought to be important for both transcriptional regulation and RNA processing. EWS can be found as part of a fusion protein with various E-twenty six (ETS) family transcription factors, most commonly Fli-1, in the Ewing sarcoma family of tumors (1-4). The amino terminus of the EWS protein, containing the transcriptional activation domain, is fused to the DNA binding domain of the ETS transcription factor, causing aberrant expression of target genes (1-5). EWS interacts with the transcription initiation complex via TFIID and RNA polymerase II subunits, as well as transcriptional regulators, such as Brn3A and CBP/p300, which suggests a role for EWS in transcriptional regulation (1,6-9). EWS also interacts with multiple components of the splicing machinery, implicating a role for EWS in RNA processing (1,10-12). EWS regulates the expression of cyclin D1, which controls G1-S phase transition during the cell cycle, at the level of transcriptional activation and mRNA splicing. The EWS-Fli-1 fusion protein has been shown to promote the expression of the cyclin D1b splice variant in Ewing sarcoma cells (13). In addition, EWS regulates the DNA damage-induced alternative splicing of genes involved in DNA repair and stress response and is required for cell viability upon DNA damage (14). Consistent with these results, EWS knockout mice display hypersensitivity to ionizing radiation and premature cellular senescence, suggesting a role for EWS in homologous recombination and maintenance of genomic stability (15).

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

Application Methods: Western Blotting

Background: RECK (reversion-inducing cysteine-rich protein with Kazal motif) is a GPI-anchored membrane glycoprotein that negatively regulates members of the matrix metalloproteinase (MMP) family and functions as a suppressor of transformation (1,2). Its function in MMP inhibition makes RECK a crucial factor in the regulation of extracellular matrix formation and stability during development (2-4). RECK has also been linked to the regulation of other extracellar matrix proteases such as ADAM10 and CD13 and functions in modulating target protein endocytosis and Notch signaling (5,6). RECK is widely expressed in normal tissue and decreased expression of RECK due to promoter methylation has been correlated with tumor transformation, angiogenesis and metastasis (1,7-9). Therefore, loss of RECK expression serves as a prognostic hallmark for cancer malignancy (10,11)

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: GLI was first identified as a gene amplified in a malignant glioma (1) capable of transforming primary cells in cooperation with adenovirus E1A (2). GLI belongs to the Kruppel family of zinc finger proteins that includes three mammalian GLI proteins: GLI1, GLI2, and GLI3 (3). These GLI proteins are similar to the Drosophila homolog Cubitus interruptus (Ci) and function as transcription factors activated by the Hedgehog signaling pathway. Hedgehog signaling plays an important role in animal development, and research studies have shown that this pathway is aberrantly activated in many types of cancers (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
REACTIVITY
Human

Background: Bromodomain-containing protein 7 (BRD7, BP75, CELTIX-1) is a conserved bromodomain-containing protein that was first identified in a screen for proteins that interact with the PDZ domain of PSD95 (1). Subsequent studies identified BRD7 as a major component of SWI/SNF chromatin remodeling complexes, where it was shown to interact directly with acetylated histones to regulate gene transcription (2,3). BRD7 also interacts with p53, and was shown to participate directly in p53-dependent transcriptional regulation (4). Loss-of-function BRD7 mutations were identified in a subset of wild-type p53 breast cancer tumor samples, implicating BRD7 as a putative tumor-suppressor of potential clinical significance (5). BRD7 also associates with the BRCA1 protein, an interaction that facilitates recruitment of BRCA1 to the ERα gene promoter (6).

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

Application Methods: Western Blotting

Background: Nijmegen breakage syndrome (NBS) is characterized by growth retardation, mental disability, immunodeficiency, defects in cell cycle checkpoints, an increased propensity for cancer, and sensitivity to ionizing radiation (1). Repair of radiation-induced DNA double-strand breaks is dependent on the multifunctional MRN complex containing Mre11, Rad50, and the NBS1 gene product p95/NBS1 (also called p95 or nibrin) (2). p95/NBS1 is a protein with a forkhead-associated domain and a BRCT repeat that regulate interaction with MDC1 and are essential for proper G2/M DNA-damage checkpoint function (3). NBS1 is critical for homologous recombination following DNA double strand breaks. This activity requires CDK-dependent association with CtIP and subsequent phosphorylation by ATM (4). ATM interacts with and phosphorylates p95/NBS1 at Ser278 and Ser343 after exposure to ionizing radiation (5,6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Members of the F-box family of proteins are characterized by the approximate 40 amino acid F-box motif named after cyclin F (1,2). F-box proteins constitute one of the four subunits of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. The substrate specificity of SCF complexes is determined by the interchangeable F-box proteins, which act as adaptors by associating with phosphorylated substrate proteins and recruiting them to the SCF core. F-box proteins contain two fundamental domains: the F-box motif mediates binding to Skp1 and a leucine rich repeat (LRR) domain mediates substrate interactions.

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: FcγRIIB (CD32B) is a low affinity, IgG Fc-binding receptor expressed on B cells, monocytes, macrophages, and dendritic cells (DCs) (1-3). It is the inhibitory Fc receptor and signals through an immunoreceptor tyrosine-based inhibitory motif (ITIM) within its carboxy-terminal cytoplasmic tail (2). Binding of immune complexes to FcγRIIB results in tyrosine phosphorylation of the ITIM motif at Tyr292 and recruitment of the phosphatase SHIP, which mediates inhibitory effects on immune cell activation (2,4). In this way, FcγRIIB suppresses the effects of activating Fc-binding receptors (3). For example, mice deficient for FcγRIIB have greater T cell and DC responses following injection of immune complexes (5, 6). In addition, FcγRIIB plays a role in B cell affinity maturation (7). Signaling through FcγRIIB in the absence of signaling through the B cell receptor (BCR) is proapoptotic, while signaling through FcγRIIB and the BCR simultaneously attenuates the apoptotic signal and results in selection of B cells with higher antigen affinity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The kindlin family of focal adhesion proteins is involved in multiple biological processes, including integrin signaling, adhesion, migration, angiogenesis, differentiation, and mitotic spindle formation (1,2). Kindlin family members 1, 2, and 3 (FERM1, FERM2, and URP2) are differentially expressed in tissues. Kindlin-1 is primarily expressed in epithelial cells, kindlin-2 is ubiquitously expressed, and kindlin-3 expression is restricted to the hematopoietic system (3).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Apoptosis mediated by death factors like FasL and TNF-α involves the formation of a death-inducing signaling complex (DISC) to their respective receptors (1). Upon ligand activation to their receptors, Fas and TNF-R1 associate with death domain (DD) containing adaptor proteins FADD (Fas associated death domain) (2,3) and TRADD (TNF-R1 associated death domain) (4). In addition to its carboxy-terminal DD, FADD contains an amino-terminal death effector domain (DED) that binds to DEDs found on caspase-8 which leads to activation of this initiator caspase (5,6). Caspase-8 subsequently activates downstream effector caspases, like caspase-3, resulting in the cleavage of proteins involved in the execution of apoptosis. Unlike FADD, TRADD does not contain a DED (4). Apoptosis driven by TNF-R1 binding to TRADD involves association of TRADD and FADD which then leads to activation of caspase-8 (7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Translation is the process where amino acid residues are assembled into polypeptides on ribosomes. This process is generally divided into three stages: initiation, elongation and termination. During elongation, mRNA and tRNA pair at the two active sites (A and P sites) on the ribosome. A number of eukaryotic elongation factors (eEFs) are involved in this process in mammalian cells (1). eEF1A, also called elongation factor Tu (EF-Tu), binds GTP and interacts with amino acyl-tRNAs to promote recruitment of amino acyl-tRNAs to the A-site of the ribosome (1). After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B (1). Studies have shown that eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXRα, RXRβ, and RXRγ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis-retinoic acid. RXRs are type-II nuclear hormone receptors that are largely localized to the nuclear compartment independent of ligand binding. Nuclear RXRs form heterodimers with nuclear hormone receptor subfamily 1 proteins, including thyroid hormone receptor, retinoic acid receptors, vitamin D receptor, peroxisome proliferator-activated receptors, liver X receptors, and farnesoid X receptor (1). Since RXRs heterodimerize with multiple nuclear hormone receptors, they play a central role in transcriptional control of numerous hormonal signaling pathways by binding to cis-acting response elements in the promoter/enhancer region of target genes (2).

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

Application Methods: Western Blotting

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

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

Application Methods: Western Blotting

Background: Nuclear protein localization protein 4 (NPL4, NPLOC4) was originally identified as a yeast nuclear transport protein that was later recognized as a critical component of the endoplasmic reticulum-associated degradation (ERAD) pathway (1,2). Mammalian NPL4 protein has an amino-terminal ubiquitin-like domain containing a p97 binding site, and a conserved carboxy-terminal zinc finger (NZF) motif responsible for binding ubiquitinated target proteins (2,3). NPL4 binds ubiquitin fusion degradation protein 1 (UFD1) to form a heterodimer that associates with the p97 AAA-ATPase, creating a protein complex that mediates delivery of ubiquitinated ER proteins to the proteasome (4,5).

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

Application Methods: Western Blotting

Background: The p21-activated kinase (PAK) family of serine/threonine kinases is engaged in multiple cellular processes, including cytoskeletal reorganization, MAPK signaling, apoptotic signaling, control of phagocyte NADPH oxidase, and growth factor-induced neurite outgrowth (1,2). Several mechanisms that induce PAK activity have been reported. Binding of Rac/Cdc42 to the CRIB (or PBD) domain near the amino terminus of PAK causes autophosphorylation and conformational changes in PAK (1). Phosphorylation of PAK1 at Thr423 by PDK induces activation of PAK1 (3). Several autophosphorylation sites have been identified, including Ser199 and Ser204 of PAK1 and Ser192 and Ser197 of PAK2 (4,5). Because the autophosphorylation sites are located in the amino-terminal inhibitory domain, it has been hypothesized that modification in this region prevents the kinase from reverting to an inactive conformation (6). Research indicates that phosphorylation at Ser144 of PAK1 or Ser139 of PAK3 (located in the kinase inhibitory domain) affects kinase activity (7). Phosphorylation at Ser21 of PAK1 or Ser20 of PAK2 regulates binding with the adaptor protein Nck (8). PAK4, PAK5, and PAK6 have lower sequence similarity with PAK1-3 in the amino-terminal regulatory region (9). Phosphorylation at Ser474 of PAK4, a site analogous to Thr423 of PAK1, may play a pivotal role in regulating the activity and function of PAK4 (10).