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Product listing: IL-2Rα/CD25 (D6K5F) Rabbit mAb, UniProt ID P01589 #13517 to Rab9 (D22A6) Rabbit mAb, UniProt ID P51151 #5133

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression including with HDACs, Rb and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also play a role as a tumor suppressors and Brg1 is mutated in several tumor cell lines (6-8).

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

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

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Interleukin-4 (IL-4) is a cytokine secreted by activated T cells, basophils, and mast cells (1,2). While it contributes to many immunomodulatory responses, it is mainly recognized as the cytokine responsible for eliciting differentiation of naive T cells into Th2 lineage cells that are defined by their secretion of IL-4, IL-5, and IL-10 (3). In addition, IL-4 contributes to immunoglobulin class switching by inducing the production of IgE from B cells (4,5). IL-4 acts through the IL-4 receptor, leading to tyrosine phosphorylation and activation of the Stat6 transcription factor (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

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

Application Methods: Western Blotting

Background: MYST1, also known as mammalian male absent on the first (MOF) and lysine acetyltransferase 8 (KAT8), is a member of the MYST (MOZ, YBF2, SAS2 and Tip60) family of histone acetyltransferases (1,2). As the catalytic subunit of two different histone acetyltransferase complexes, MSL and NSL, MYST1 is responsible for the majority of histone H4 lysine 16 acetylation in the cell. MYST1 also acetylates p53 on lysine 120 and is important for activation of pro-apoptotic genes (1,2). As a component of the MSL complex, MYST1 associates with MSL1, MSL2L1, and MSL3L1, and specifically acetylates histone H4 on lysine 16 (3-5). As part of the NSL complex, MYST1 associates with the MLL1 histone methyltransferase complex containing MLL1/KMT2A, ASH2L, HCFC1, WDR5 and RBBP5, and shows broader acetyltransferase activity for histone H4 on lysines 5, 8, and 16 (3-5). MYST1 plays a critical role in the regulation of transcription, DNA repair, autophagy, apoptosis, and emybryonic stem cell pluripotency and differentiation (1,2,6). Loss of MYST1 leads to a global reduction in histone H4 lysine 16 acetylation, a common hallmark found in many human cancers. A reduction of MYST1 protein levels and histone H4 lysine 16 acetylation is associated with poor prognosis in breast, renal, colorectal, gastric, and ovarian cancers (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: SMG-1 is a member of the phosphoinositide 3-kinase-related kinase (PIKK) family, which includes ATM, ATR, mTOR, DNA-PKcs, and TRRAP (1,2). Activated by DNA damage, SMG-1 has been shown to phosphorylate p53 and hUpf1 (SMG-2) (1-4). hUpf1 is a subunit of the surveillance complex that allows degradation of messenger RNA species containing premature termination codons (PTCs). This process, known as nonsense-mediated mRNA decay (NMD), prevents the translation of truncated forms of proteins that may result in gain of function or dominant negative species. NMD occurs under normal cellular conditions as well as in response to damage (5,6). SMG-1 has also been shown to affect cell death receptor signaling and to protect cells from extrinsically induced apoptotic cell death (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: NADP+ dependent methylenetetrahydrofolate dehydrogenase 1-like (MTHFD1L) is a mitochondrial enzyme that catalyzes the production of formate from 10-formyl-tetrahydrofolate, the last step in one-carbon (1-C) flow from mitochondria to cytoplasm (1,2). These one-carbon end products are required for de novo synthesis of thymidylate and purines. In the mitochondria, these essential one-carbon products are formed by a series of reactions catalyzed by a pair of enzymes (MTHFD2 and MTHFD1L), but by the trifunctional MTHFD1 enzyme in the cytoplasm (3). The 10-formyl-tetrahydrofolate synthetase MTHFD1L is widely expressed in most adult tissues and at all stages of mammalian embryonic development (1). Research studies using MTHFD1L knockout mice indicate that MTHFD1L plays an essential role in neural tube formation; mice lacking MTHFD1L displayed neural tube and craniofacial defects leading to embryonic lethality (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CD8+ cytotoxic T cells recognize peptides presented by MHC class I molecules on the surface of infected cells and tumor cells. The transporters associated with antigen processing 1 and 2 (TAP1 and TAP2) form the TAP complex which resides on the ER membrane and transports peptides from the cytoplasm into the ER for loading onto MHC class I molecules (1-8). In addition, TAP localized to endosomal membranes is important for cross-presentation by dendritic cells (9,10). IFN-γ produced by T cells and NK cells in response to infection causes upregulation of TAP1 and TAP2, resulting in increased antigen presentation to T cells (11). Some viral proteins inhibit TAP function or downregulate TAP expression resulting in viral immune evasion (12,13). In addition, investigators have observed reduced TAP expression in a variety of tumor types, and it is thought to be one mechanism for tumor immune evasion (14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Forkhead box protein A1 (FoxA1, HNF3α) is a transcription factor required for the development of endoderm-derived organs, such as liver, lung, and prostate (1). FoxA1 functions as a pioneer factor that is recruited primarily to the distant enhancers to change chromatin structure for transcription in a cell type-specific manner (2,3). The FoxA1 transcription factor is implicated in various diseases, playing a role in hormone-dependent disorders such as breast and prostate cancers (4). The treatment of relapsing-remitting multiple sclerosis patients with IFN-β results in FoxA1-induced stimulation of a novel population of FoxA1(+) regulatory T-cells, suggesting a possible immunosuppressive role for FoxA1 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Malate dehydrogenase (MDH) is a key enzyme in the tricarboxylic acid cycle and malate/aspartate shuttle (1,2). MDH is widely expressed in organisms from most bacteria to all eukaryotes (2). The cytoplasmic MDH isoenzyme (cMDH or MDH1) primarily reduces oxaloacetate to malate in the malate/aspartate shuttle (1-3). The major function of the mitochondrial MDH isoenzyme (mMDH or MDH2) is to oxidize malate to oxaloacetate in the tricarboxylic acid cycle (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CARD9 is a caspase recruitment domain (CARD)-containing adaptor protein expressed by myeloid cells (1,2). It is required for antifungal immunity downstream of pathogen detection by C-type lectin receptors (CLRs) such as Dectin-1 (3,4). Recognition of carbohydrates on fungal cell walls by CLRs leads to activation of the tyrosine kinase Syk, followed by activation of PKCδ (5,6). PKCδ phosphorylates CARD9, enabling the assembly of a complex containing CARD9 and Bcl10 (6). This complex activates NF-κB, resulting in upregulation of inflammatory cytokines important for initiation of adaptive immunity (3,4,6,7). CARD9 was also shown to be important for the induction of IL-1β, downstream of the viral nucleic acid sensor RIG-I, as well as for the generation of reactive oxygen species important for bacterial killing by macrophages (2,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).

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

Application Methods: Western Blotting

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitin regulatory X domain-containing protein 8 (UBXD8, also known as ETEA and FAF2) is a hairpin-anchored endoplasmic reticulum (ER) protein involved in ER associated degradation (ERAD). It influences this process by promoting translocation of misfolded proteins from the ER lumen to the cytoplasm for proteasome-mediated degradation (1). UBXD8 is a sensor for unsaturated fatty acids. In the absence of fatty acids UBXD8 binds to and targets INSIG1 for degradation, ultimately resulting in activation of SREBP-1. Under this condition, UBXD8 also inhibits triglyceride synthesis by blocking the conversion of diacylglycerols into triglycerides. Unsaturated fatty acids trigger UBXD8 polymerization and dissociation of UBXD8/INSIG1 complex, leading to feedback inhibition of SREBP-1 (2, 3). This induces UBXD8 to translocate from the ER to lipid droplets, where it binds to ATGL and inhibits its lipase activity (4, 5). The complex containing p97 and UBXD8 is reported to promote disassembly of the ribonucleoprotein complex to control mRNA stability (6). In addition, UBXD8 binds to and promotes degradation of neurofibromin (NF1), suggesting a role in regulating Ras activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex is a critical regulator of cell growth (1,2). Its activity is modulated by energy levels, growth factors, and amino acids via signaling through Akt, MAPK, and AMPK pathways (3,4). Recent studies found that the four related GTPases, RagA, RagB, RagC, and RagD, interact with raptor within the mTORC1 complex (1,2). These interactions are both necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: NKX3.1 is a homeobox transcription factor that in mammals plays a defining role in embryonic prostate morphogenesis. The expression of mammalian NKX3.1 is androgen-dependent, restricted primarily to developing and mature prostate epithelium, and is frequently reduced or lost in prostate cancer (1-3). The human NKX3.1 gene is located on chromsome 8p21.2, within a region that shows loss of heterozygosity (LOH) in >50% of prostate cancer cases (2). Allelic loss at the NKX3.1 locus is also common in high grade Prostate Intraepithelial Neoplasia (PIN), thought to be a putative precursor lesion to invasive prostate adenocarcinomas, suggesting that LOH at the NKX3.1 locus is a critical early step in prostate cancer development (4). Notably, the remaining NKX3.1 allele is intact in the majority of LOH cases, leading to the suggestion that NKX3.1 functions as a haploinsufficient tumor suppressor (4-6). Due to its highly restricted expression in prostate epithelial cells, NKX3.1 has been suggested as a diagnostic marker of prostate carcinoma (7), and may have additional utility as a biomarker of metastatic lesions originating in the prostate (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Hemoglobin (Hb, Hgb) is a heme-containing transport protein found primarily in the red blood cells of humans and most other vertebrates. The primary function of hemoglobin is to transport oxygen from the external environment to the body tissues. Hemoglobin also facilitates metabolic waste removal by assisting in the transport of carbon dioxide from tissues back to the respiratory organs (1). Mature hemoglobin is a tetrameric protein complex, with each subunit containing an oxygen-binding heme group (2). Multiple isoforms of hemoglobin exist, which vary in relative abundance depending on developmental stage. Adult hemoglobin (HbA) is comprised of two α subunits and two β subunits and is the predominant hemoglobin found in red blood cells of children and adults. Fetal hemoglobin (HbF) contains two α subunits and two γ subunits and is the predominant isoform found during fetal and early postnatal development (2,3). Mutations that alter the structure or abundance of specific globin subunits can result in pathological conditions known as hemoglobinopathies (4). One such disorder is sickle cell disease, which is characterized by structural abnormalities that limit the oxygen carrying capacity of red blood cells. By contrast, thalassemia disorders are characterized by deficiencies in the abundance of specific hemoglobin subunits (4). Clinical treatments that are designed to alter the expression of specific hemoglobin subunits can be used to treat hemoglobinopathies (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The Phosphatase of Regenerating Liver (PRL) family is a distinct group of protein tyrosine phosphatases (PTP), containing a signature phosphatase domain but otherwise lacking homology to known PTP proteins. There are currently three known members of the PRL family (PRL1-3). PRL-1 was the first family member to be identified; it was initially characterized as an immediate early gene (IEG) in regenerating liver and mitogen-treated fibroblasts (1). PRL-3, known widely as PTP4A3, is now the most well-characterized member of the PRL family, due to its important role in regulating cell proliferation, and possibly cancer metastasis. While specific substrates of the PRL-family proteins have remained largely undefined, a recent study in colon cancer cell lines reported that PTP4A3 dephosphorylated integrin β1 at Tyr783 (2). PTP4A3 was also shown to play a potential role in the progression of cardiac hypertrophy by inhibiting tyrosine phosphorylation of the docking protein p130 (3). Increased rates of both cell proliferation and motility have been observed in immortalized cell lines and murine lung tumor cells over-expressing PTP4A3 (3,4), and elevated levels of PTP4A3 protein are associated with a subset of human cancers (5,6).

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

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

Background: Succinyl-CoA synthetase α subunit (SUCLG1) catalyzes the conversion of succinate to succinyl-CoA and plays a key role in the citric acid cycle (1,2). Deficiency of this enzyme leads to a variety of diseases including fatal infantile lactic acidosis (3) and mitochondrial hepatoencephalomyopathy (4).

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

Application Methods: Immunoprecipitation, 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

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

Background: PTK6/BRK (protein-tyrosine kinase 6, Breast Tumor Kinase) is a non-receptor tyrosine kinase that is closely related to the FRK family of kinases and distantly related to SRC family kinases (1). PTK6/BRK possesses an N-terminal SRC homology 3 (SH3) domain that regulates kinase-substrate interactions, an auto-inhibitory SRC homology 2 (SH2) domain, and a carboxy-terminal kinase domain. Phosphorylation at Tyr342 in the activation loop of the kinase domain upregulates kinase activity, whereas phosphorylation at Tyr447 inhibits kinase activity (2). PTK6/BRK is expressed in differentiated epithelial cells in normal skin, gastrointestinal tract and colon, and its expression level is reportedly upregulated in some cancer cell types, including breast carcinoma, prostate cancer and colon cancer (3-5). Although typically localized in the nucleus of normal cells, PTK6/BRK has also been observed in the cytosol and plasma membrane in some contexts, notably during tumor progression, where it likely interacts with unique substrates. In the nucleus, PTK6/BRK functions to mediate signaling events important for differentiation and apoptosis (4); outside the nucleus, PTK6/BRK may function to relay upstream RTK signaling to downstream pathways via phosphorylation and activation of substrates such as paxillin, STAT and AKT, which in turn activate pathways to promote cell survival, invasion and migration. The upregulation, altered subcellular localization and associated signaling functions of PTK6/BRK in tumor cells make it a promising target for cancer therapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Mammalian alkaline phosphatases (APs) are highly conserved zinc-containing allosteric enzymes that are able to hydrolyze and transphosphorylate a wide range of compounds (1). There are four known human alkaline phosphatase isozymes: TNAP (tissue-nonspecific; bone/liver/kidney), ALPP (placental), ALPP2 (germ cell), and ALPI (intestinal) (2). Placental alkaline phosphatase (ALPP) is bound to the plasma membrane via a glycosyl-phosphatidylinositol (GPI) anchor (3). It is expressed primarily in the placenta (4) and may be involved in transplacental IgG transport (5). ALPP has been found to be overexpressed on the surface of several different types of solid tumor cells (6) and elevated serum concentrations of ALPP and ALPP-like enzymes has been found to be associated with ovarian, cervical, and testicular cancer (7).

$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, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Postsynaptic Density Protein 93 (PSD93) is a member of the PSD subfamily of the membrane-associated guanylate kinase (PSD-MAGUK) proteins. Structurally, it most closely resembles PSD95, consisting of an N-terminal variable segment followed by three PDZ domains, an SH3 domain, and an inactive guanylate kinase (GK) domain (1,2). PSD93 is expressed in neuronal cells and located at the synapse where it interacts with neuronal receptors and proteins including the NMDA receptor (2-4), K+ channels (5,6), and the AMPA receptor (7) to regulate their membrane localization and neuronal signaling. Research studies have implicated PSD93 in postsynaptic related persistent pain induction, making PSD93 a potential target for treatment of this syndrome (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (4,5). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (6-8). Lamin B1 is also cleaved by caspases during apoptosis (9). Research studies have shown that duplication of the lamin B1 gene LMNB1 is correlated with pathogenesis of the neurological disorder adult-onset leukodystrophy (10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The human WSTF gene is located within the common Williams Syndrome (WS) deletion area at chromosome 7q11.23. Several WSTF gene products have been detected with little difference in length of polypeptides (1-3). Functional motifs identified by sequence-homology searches include a PHD-type zinc finger motif followed by a bromodomain. Both motifs are found in many transcription factors, suggesting that WSTF may function as a transcription factor. A Drosophila gene (acf1) was cloned, which encodes two forms of Acf1 proteins with molecular weight 170 kDa and 185 kDa, respectively (4). It was demonstrated that Acf1 is structurally related to the human WSTF gene. Acf1 forms a complex with another protein, ISWI, and functions in the ATP-dependent catalysis of chromatin assembly (4).

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

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

Background: Eps15 (EGFR pathway substrate 15) was originally discovered as a substrate for the kinase activity of EGFR (1). Eps15 has a tripartite structure comprising an amino terminal portion, which contains three evolutionarily conserved EH protein-protein interaction domains, a central putative coiled-coil region required for constitutive oligmerization, and a carboxy terminal domain containing multiple copies of the amino acid triplet Asp-Pro-Phe that constitute the AP2 binding domain. The carboxy terminal domain also contains two ubiquitin interaction motifs (UIMs), the last of which is indespensible for Eps15 binding to ubiquitin (1). Several lines of evidence support a role for Eps15 in clathrin-mediated endocytosis, including the endocytosis of synaptic vesicles. Eps15 binds to AP2 as well as other proteins involved in endocytosis and/or synaptic vesicle recycling, such as synaptojanin1 and epsin. Furthermore, Eps15 colocalizes with markers of the plasma membrane clathrin-coated pits and vesicles (2). Eps15 regulates the endosomal trafficking of c-Met (3) and EGFR (4), possibly by recruiting the ubiquitinated receptors to the rims of clathrin-coated pits through interaction between the ubiquitin tag and its UIMs.The EPS15 gene yields two isoforms that are believed to reside in distinct subcellular locations and are thus implicated in different facets of endosomal trafficking (5). Human EPS15 has been mapped to chromosome 1p31-p32, a region displaying several nonrandom chromosomal abnormalities, including deletions in neuroblastoma and translocations in acute lymphoblastic and myeloid leukemias. Research has shown two translocations t(1;11)(p32;q11) are found in rare cases of myeloid leukemia where the Eps15 gene was fused to the HRX gene, resulting in two reciprocal fusion genes (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin-like growth factor (IGF) signaling plays a major role in regulating the proliferation and metabolism of normal and malignant cells. Insulin-like growth factor-binding proteins (IGFBPs) play an integral role in modifying IGF actions in a wide variety of cell types. The six IGFBP family members share a high affinity for IGF binding and are structurally related, but are encoded by distinct genes (1). IGF binding proteins can exert stimulatory or inhibitory effects by controlling IGF availability through high affinity binding of IGF at the carboxy-terminal domain (2,3). IGFBP3 is the most abundant serum IGF binding protein and the main mediator for IGF-I bioactivities. IGFBP3 also binds IGF-II, insulin, and other cellular and extracellular components to regulate cell growth, development, and apoptosis through both IGF-dependent and IGF-independent mechanisms (4-8). Research studies describe correlations between increased IGF-I levels and reduced levels of IGFBP3 with increased risks of developing cancer, including breast, colon, lung, and prostate cancer (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Rab7 and Rab9 are members of the Ras superfamily of small Rab GTPases (1). Both proteins are located in late endosomes, but exert different functions. Rab7 associates with the RIPL effector protein to control membrane trafficking from early to late endosome and to lysosomes (2,3). Rab7 also helps to regulate growth receptor endocytic trafficking and degradation (3,4), and maturation of phagosome and autophagic vacuoles (4-6). Rab9 interacts with its effector proteins p40 and TIP47 (7,8) to promote the MPR (mannose 6-phosphate receptor)-associated lysosomal enzyme transport between late endosomes and the trans Golgi network (9,10).