Microsize antibodies for $99 | Learn More >>

Product listing: Hexokinase II Antibody, UniProt ID P52789 #2106 to eIF3C Antibody, UniProt ID Q99613 #2068

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Hexokinase catalyzes the conversion of glucose to glucose-6-phosphate, the first step in glycolysis. Four distinct mammalian hexokinase isoforms, designated as hexokinase I, II, III, and IV (glucokinase), have been identified. Hexokinases I, II, and III are associated with the outer mitochondrial membrane and are critical for maintaining an elevated rate of aerobic glycolysis in cancer cells (Warburg Effect) (1) in order to compensate for the increased energy demands associated with rapid cell growth and proliferation (2,3).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

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

Application Methods: Western Blotting

Background: Secretory proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones, including Grp94, to help ensure correct protein folding. Grp94 is a glucose-regulated protein (1) with sequence homology to Hsp90 (2). In addition to its role in helping to facilitate folding of a number of secretory proteins to their correct conformation (3), studies suggest that Grp94 derived from cancer cells also induces anti-tumor immune responses in mouse tumor models (4, 5). One way in which Grp94 promotes tumor immunogenicity is its ability to bind to and present tumor-derived peptides as antigens (6). Furthermore, Grp94 has also been shown to induce maturation of dendritic cells (7). Taken together, Grp94 functions both as a tumor-specific antigen and as an activator of antigen-presenting cells to elicit an anti-cancer immune response (8).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$260
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).

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

Application Methods: 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) (1). RhoA, RhoB and RhoC are highly homologous, but appear to have divergent biological functions. Carboxy-terminal modifications and differences in subcellular localization allow these three proteins to respond to and act on distinct signaling molecules (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Stem cell factor (SCF) is a growth factor that is essential for hematopoiesis, melanogenesis and fertility. SCF is also known as mast cell growth factor (MCGF), steel factor (SLF), or kit ligand (KL) (1-3). SCF mediates its biological effects by binding to and activating c-Kit (4). SCF induces dimerization of c-Kit followed by trans-autophosphorylation of the cytoplasmic protein tyrosine kinase domain, leading to subsequent recruitment of signaling proteins, tyrosine phosphorylation of substrates and activation of multiple signaling pathways (5,6). SCF/c-Kit may take part in the growth control of human malignancies (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Centrins are small conserved microtubule nucleating proteins localized to centrosomes, also known as microtubule organizing centers (MTOC), in eukaryotic cells. Centrin-1 is associated with cells that have cilia and flagella, whereas centrin-2 and -3 are ubiquitously expressed and important in centrosome duplication during cell division, as well as the structure and function of the MTOC (1-3). Human centrin-2 has also been shown to localize to nuclear pores and to have a role in regulation of mRNA export (4). The yeast ortholog of centrin-2, CDC31, plays a part in control of protein degradation and sensitivity to DNA damage (5).

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

Application Methods: Western Blotting

Background: CDK-activating kinase (CAK) is a complex of CDK7 and cyclin H. The complex is involved in cell cycle regulation by phosphorylating an activating residue in the T-loop domain of cdks (1). Regulation of CAK activity is mediated by T-loop phosphorylation and by association with MAT1, both of which enhance its kinase activity toward the CTD of RNA polymerase II (2,3) and other substrates such as p53 (4). CAK is an essential component of the transcription complex TFIIH and may interact directly with TFIIH helicases (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The MCF2/Dbl proto-oncogene product is the founding member of the Dbl family of Rho guanine nucleotide exchange factors (GEFs) that are characterized by their Dbl homology (DH) domain (1). GEFs stimulate the formation of the active, GTP-bound form of small GTPases such as Rho, Rac and Cdc42, signaling to various downstream molecules and regulating diverse cell functions. While the overexpressed, full-length Dbl gene has transforming activity (2), mutations resulting in truncated Dbl cause the protein to become highly oncogenic. This truncated form of Dbl, which lacks the amino-terminal 497 amino acids, has constitutive GEF activity (3) and is more stable than the full-length variant (4), allowing for increased signaling to downstream effector molecules.Dbl interacts with ezrin, a member of the ezrin/radixin/moesin (ERM) family of proteins that links the plasma membrane to the actin cytoskeleton. Dbl interacts with ezrin in lipid microdomains, which leads to Cdc42 activation and the regulation of processes such as filopodia formation and cell polarity (5,6). Dbl localization and biological activities are regulated in part by phosphatidylinositol 3-kinase (PI3K) (7). Dbl is also involved in cell survival and inhibits apoptosis through induction of Akt phosphorylation at Thr308 (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The LEDGF (lens epithelium-derived growth factor) gene encodes splice variants P75 and P52 (1). LEDGF (C57G11) Rabbit mAb detects the 75 kDA LEDGF splice form. Both LEDGF variants have transcriptional coactivator functions that may regulate gene transcription and mRNA splicing of a variety of proteins that are essential for cell growth and survival. (2,3). LEDGF has also been identified as a factor that can, in serum free media, stimulate the growth and survival of lens epithelial cells and other cell types such as retinal photoreceptor cells, COS7 cells, skin fibroblasts, and keratinocytes (2). In addition to its function as a transcriptional coactivator, LEDGF has been shown to be involved in the pathogenesis of atopic dermatitis (4) and in the activity of HIV1 integrase. LEDGF binds chromatin throughout the cell cycle, and may act as a chromatin docking factor for HIV integrase and other lentiviral pre-integration complexes. It protects HIV integrase from degradation, and influences the pattern of viral integration into the cell genome (5).

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

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

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$380
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The epidermal growth factor (EGF) receptor is a 170 kDa transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Research studies have shown that somatic mutations in the tyrosine kinase domain of EGF receptor (EGFR) are present in a subset of lung adenocarinomas that respond to EGFR inhibitors, such as gefinitib and erlotinib (1-3). Two types of mutations account for approximately 90% of mutated cases: a specific point mutation, L858R, that occurs in exon 21 and short in-frame deletions in exon 19 (4,5). The most frequent exon 19 deletion is E746-A750, accounting for 90% of lesions at this site, although some rare variants occur.

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

Application Methods: Western Blotting

Background: The regulatory associated protein of mTOR (Raptor) was identified as an mTOR binding partner that mediates mTOR signaling to downstream targets (1,2). Raptor binds to mTOR substrates, including 4E-BP1 and p70 S6 kinase, through their TOR signaling (TOS) motifs and is required for mTOR-mediated phosphorylation of these substrates (3,4). Binding of the FKBP12-rapamycin complex to mTOR inhibits the mTOR-raptor interaction, suggesting a mechanism for rapamycin's specific inhibition of mTOR signaling (5). This mTOR-raptor interaction and its regulation by nutrients and/or rapamycin is dependent on a protein called GβL (6). GβL is also part of the rapamycin-insensitive complex between mTOR and rictor (rapamycin-insensitive companion of mTOR), and may mediate rictor-mTOR signaling to downstream targets including PKCα (7). Furthermore, the rictor-mTOR complex has been identified as the previously elusive PDK2 responsible for the phosphorylation of Akt/PKB on Ser473, facilitating phosphorylation of Akt/PKB on Thr308 by PDK1 and required for the full activation of Akt/PKB (8).Recently raptor has been identified as a direct substrate of the AMP-activated protein kinase (AMPK) (9). AMPK phosphorylates raptor on Ser722/Ser792 (9). This phosphorylation is essential for inhibition of the raptor-containing mTOR complex 1 (mTORC1) and induces cell cycle arrest when cells are stressed for energy (9). These findings suggest that raptor is a critical switch that correlates cell cycle progression with energy status.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: La antigen is recognized by antibodies in patients with autoimmune disorders such as systemic lupus erythematosus and Sjögren's syndrome (1). La antigen binds to the 5'-noncoding region of poliovirus RNA and is an IRES trans-acting factor (1,2). Depletion of La antigen reduces the function of poliovirus IRES in vivo (3). La antigen, when phosphorylated at Ser366, has been shown to associate with nuclear precursor tRNAs and facilitate their processing (4). The nonphosphorylated La antigen interacts with the mRNAs that have 5'-terminal oligopyrimidine (5'TOP) motifs to control protein synthesis (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The carboxy terminus of Hsc70-interacting protein (CHIP, STUB1) is a co-chaperone protein and functional E3 ubiquitin ligase that links the polypeptide binding activity of Hsp70 to the ubiquitin proteasome system (1). Cytoplasmic CHIP protein contains three 34-amino acid TPR (tetratricopeptide repeat) domains at its amino terminus and a carboxy-terminal U-box domain. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, while E3 ubiquitin ligase activity is confined to the U-box domain (2,3). The binding of CHIP to Hsp70 can stall the folding of Hsp70 client proteins and concomitantly facilitate the U-box dependent ubiquitination of Hsp70-bound substrates (4-6). CHIP appears to play a central role in cell stress protection (7) and is responsible for the degradation of disease-related proteins that include cystic fibrosis transmembrane conductance regulator (4), p53 (8), huntingtin and Ataxin-3 (9), Tau protein (10), and α-synuclein (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germline stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and Homo sapiens (1). Both Miwi and Mili proteins are mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mice (3-5).

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

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: TMP21, a type I transmembrane protein, is a member of the p24 cargo protein family, which is highly enriched in the ER, the Golgi and coat protein (COP) I and II transport vesicles (1,2). TMP21 is involved in protein transport and vesicular targeting. In particular, TMP21 influences APP trafficking by stabilizing nascent APP. The absence of TMP21 leads to enhanced maturation and cell surface accumulation of APP (3). In addition, TMP21 is a non-essential component of the γ-secretase complex with the potential to modulate γ-secretase mediated cleavage and Aβ production without having an effect on ε-secretase activity (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Mena (mammalian enabled), EVL, and VASP are members of the Ena/VASP family, which is involved in controlling cell shape and cell movement by shielding actin filaments from capping proteins (1). Ena/VASP proteins have three specific domains: an amino-terminal EVH1 domain controlling protein localization; a central proline-rich domain mediating interactions with both SH3 and WW domain containing proteins, including profilin; and a carboxy-terminal domain causing tetramerization and binding to actin (2). Mena interacts with actin filaments at the growing ends localizing to lamellipodia and to tips of growth cone filopodia in neurons. Axons projecting from interhemispheric cortico-cortical neurons are misrouted in newborn, homozygous Mena knock-out mice (3). Mena is phosphorylated at Ser236 by PKA, thereby promoting filopodial formation and elongation in the growth cone (4).Three forms of Mena corresponding to 80, 88 and 140 kD are known. The 80 kD protein is broadly expressed in contrast to the 140 kD protein which is enriched in neural cell types. Alternative splicing produces these forms. The 88 kD protein is mainly found in embryonic cell types and is likely the result of post-translational modification. Expression of all three forms is completely eliminated in Mena homozygous mutant animals (1, 3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Naked1 (Nkd1) and Naked2 (Nkd2) are homologs of Drosophila Naked cuticle, a negative regulator of Wnt/Wingless signaling pathway which functions through a feedback mechanism (1,2). Both Drosophila and vertebrate Naked proteins contain a putative calcium-binding EF-hand motif, however, Drosophila Naked binds to zinc instead of calcium (3). Naked inhibits the canonical Wnt/β-catenin pathway by binding to Dishevelled proteins and directs Dishevelled activity towards the planar cell polarity pathway (2,4). Naked1 is a direct target of Wnt signaling and is overexpressed in some colon tumors due to constitutive activation of Wnt/β-catenin pathway (5). Naked2 is myristoylated and is required for sorting of TGF-α to the basolateral plasma membrane of polarized epithelial cells (6).

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

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germ-line stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and human (1). Miwi and Mili proteins are both mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mouse (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: DLK1 (delta-like-1), also known as fetal antigen 1 (FA1) and preadipocyte factor 1 (pref-1), is a member of the epidermal growth factor (EGF)-like family of proteins, containing six tandem EGF-like repeats (1,2). DLK1 is a paternally expressed, imprinted gene that plays an important role in normal development and in the maintenence of homeostasis of adipose tissue mass (3). DLK1 deficient mice display growth retardation, obesity, skeletal malformation, and increased serum lipid metabolites (4). It has been reported that the ectodomain of DLK1 is shredded from the cell surface and inhibits adipocyte differentiation ( 5-7).

$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).