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Product listing: FoxP3 (D6O8C) Rabbit mAb, UniProt ID Q9BZS1 #12632 to Galectin-3/LGALS3 (D4I2R) XP® Rabbit mAb, UniProt ID P17931 #87985

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), which lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer, and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), which lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer, and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Frizzled (Fzd) belongs to the seven transmembrane-spanning G-protein-coupled receptor (GPCR) superfamily (1). Fzds have a large extracellular N-terminal region containing a cysteine-rich domain (CRD), which is involved in binding to Wnt proteins (1,2). The intracellular C-terminus binds to the PDZ domain of Dvl proteins, a major signaling component downstream of Fzd (3). Wnt proteins bind to Fzd and the co-receptors LRP5 or LPR6, and activate Wnt/β-catenin pathway through inhibiting phosphorylation of β-catenin by GSK3-β (4,5). In addition to this canonical Wnt/β-catenin pathway, some Wnt proteins can also activate the Fzd/Ca2+ pathway and Fzd/PCP (planar cell polarity) pathway (6,7). The mammalian Fzd subfamily has 10 members (Fzd1 to Fzd10) and they may mediate signaling through different pathways (8). Some Fzds can also bind to other secreted proteins, like Norrin and R-Spondin (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Frizzled (Fzd) belongs to the seven transmembrane-spanning G-protein-coupled receptor (GPCR) superfamily (1). Fzds have a large extracellular N-terminal region containing a cysteine-rich domain (CRD), which is involved in binding to Wnt proteins (1,2). The intracellular C-terminus binds to the PDZ domain of Dvl proteins, a major signaling component downstream of Fzd (3). Wnt proteins bind to Fzd and the co-receptors LRP5 or LPR6, and activate Wnt/β-catenin pathway through inhibiting phosphorylation of β-catenin by GSK3-β (4,5). In addition to this canonical Wnt/β-catenin pathway, some Wnt proteins can also activate the Fzd/Ca2+ pathway and Fzd/PCP (planar cell polarity) pathway (6,7). The mammalian Fzd subfamily has 10 members (Fzd1 to Fzd10) and they may mediate signaling through different pathways (8). Some Fzds can also bind to other secreted proteins, like Norrin and R-Spondin (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: FERM domain-containing protein 6 (FRMD6, Willin) belongs to the 4.1 superfamily, a group of proteins characterized by the presence of a Band 4.1, Ezrin, Radixin, Moesin (FERM) domain in the amino-terminal region (1). Members of this protein superfamily, which also includes Merlin, Ezrin, Radixin, Moesin and Talin, function primarily as adaptor proteins that link plasma membrane-associated proteins to the actin cytoskeleton (2). FRMD6 is considered orthologous to the Drosophila Expanded (Ex) protein, which is a 4.1 family protein that functions together with Merlin and Kibra to regulate Hippo signaling, upstream of the Salvador/Warts/Hippo core kinase cassette (3). Research studies suggest a similar role for FRMD6 in regulating the Hippo pathway in mammals. For example, ectopic expression of FRMD6 leads to increased phosphorylation of MST1/2, LATS1, and YAP, which is indicative of Hippo pathway activation. Loss of FRMD6 expression in MCF10A cells induces a phenotype change resembling epithelial-mesenchymal transition (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Formimidoyltransferase-cyclodeaminase (FTCD) catalyzes two key consecutive reactions in the histidine degradation pathway and links histidine catabolism to one-carbon metabolism. It converts tetrahydrofolate (THF) to 5, 10-methenyl-THF (1,2). Loss of FTCD decreases the sensitivity of cancer cells to chemotherapeutic drug methotrexate, an inhibitor of dihydrofolate reductase (DHFR). DHFR reduces dihydrofolate to tetrahydrofolate, an essential cofactor for nucleotide biosynthesis. Lack of FTCD leads to higher levels of tetrahydrofolate in methotrexate-treated cells, therefore reducing the effect of methotrexate. Conversely, greater depletion of tetrahydrofolate by FTCD through enhanced histidine degradation pathway may boost the efficacy of methotrexate (3,4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Ferritin (FTH) is a ubiquitous and highly conserved protein which plays a major role in iron homeostasis by sequestering and storing iron in a non-toxic and bioavailable form (1). The assembled ferritin molecule, often referred to as a nanocage, can store up to 4,500 atoms of iron (2,3). It forms a holoenzyme of ~450 kDa, consisting of 24 subunits made up of two types of polypeptide chains: ferritin heavy chain and ferritin light chain, each having unique functions. Ferritin heavy chains catalyze the first step in iron storage, the oxidation of Fe(II), whereas ferritin light chains promote the nucleation of ferrihydrite, enabling storage of Fe(III) (4). In addition to iron buffering, heavy chain ferritin also enhances thymidine biosynthesis (5). Serum ferritin levels serve as an indicator of the amount of iron stored in the body. Serum ferritin is the most sensitive test for anaemia. The level of serum ferritin is markedly elevated in inflammation, malignancy, and iron overload disorders (6). Research studies have found that defects in ferritin proteins are also associated with several neurodegenerative diseases (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: FTO (fat mass and obesity-associated protein) is the first obesity gene product identified by genome-wide association studies and it is associated with the largest effect size for this class of proteins (1-4). Multiple single-nucleotide polymorphisms (SNPs) in the first intron of the FTO gene have been associated with increased body weight and obesity. Further studies reported that FTO risk alleles were associated with an increase in energy intake, a reduction of activity, and possibly an increased daily fat intake (4).FTO is a DNA and RNA demethylase that catalyzes the oxidative demethylation of thymidine and uracil. Among its targets is an mRNA subset involved in regulation of learning, reward behavior, motor functions, and feeding (5). Loss of the FTO gene in mice leads to postnatal growth retardation and a significant reduction in adipose tissue. Mice deficient in the FTO gene have lean body mass due to increased energy expenditure and systemic activation of sympathetic neurons, while overexpression of FTO in mice leads to increased food intake and results in obesity. These results demonstrate that FTO is functionally involved in energy homeostasis (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: FTO (fat mass and obesity-associated protein) is the first obesity gene product identified by genome-wide association studies and it is associated with the largest effect size for this class of proteins (1-4). Multiple single-nucleotide polymorphisms (SNPs) in the first intron of the FTO gene have been associated with increased body weight and obesity. Further studies reported that FTO risk alleles were associated with an increase in energy intake, a reduction of activity, and possibly an increased daily fat intake (4).FTO is a DNA and RNA demethylase that catalyzes the oxidative demethylation of thymidine and uracil. Among its targets is an mRNA subset involved in regulation of learning, reward behavior, motor functions, and feeding (5). Loss of the FTO gene in mice leads to postnatal growth retardation and a significant reduction in adipose tissue. Mice deficient in the FTO gene have lean body mass due to increased energy expenditure and systemic activation of sympathetic neurons, while overexpression of FTO in mice leads to increased food intake and results in obesity. These results demonstrate that FTO is functionally involved in energy homeostasis (6-8).

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

Application Methods: Western Blotting

Background: Fumarate hydratase (Fumarase, FH) is canonically regarded as a mitochondrial enzyme of the tricarboxylic acid cycle that catalyzes fumarate to malate (1,2). Studies have demonstrated that deficiencies in FH can lead to hereditary leiomyomatosis and renal cell cancer (1,3) or, in homozygous germline mutations, severe neurological and muscular disorders (1,2). There also exists a cytosolic fumarase isoenzyme that is involved in DNA damage repair (3).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fragile X syndrome is a genetic disorder characterized by a spectrum of physical and behavioral features and is a frequent form of inherited mental retardation (1). X-linked FMRP (FMR-1) and its two autosomal homologs, FXR1 and FXR2, are polyribosome-associated RNA-binding proteins that are involved in the pathogenesis of fragile X syndrome (1-3). Each of the fragile X proteins can self-associate, as well as form heteromers with the other two related proteins (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). The Drosophila homolog of FMRP (dFMRP) associates with Argonaute 2 (Ago2) and Dicer and can coimmunoprecipitate with miRNA and siRNA (5). These results suggest that fragile X syndrome is related to abnormal translation caused by defects in RNAi-related pathways. In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fragile X syndrome is a genetic disorder characterized by a spectrum of physical and behavioral features and is a frequent form of inherited mental retardation (1). X-linked FMRP (FMR-1) and its two autosomal homologs, FXR1 and FXR2, are polyribosome-associated RNA-binding proteins that are involved in the pathogenesis of fragile X syndrome (1-3). Each of the fragile X proteins can self-associate, as well as form heteromers with the other two related proteins (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). The Drosophila homolog of FMRP (dFMRP) associates with Argonaute 2 (Ago2) and Dicer and can coimmunoprecipitate with miRNA and siRNA (5). These results suggest that fragile X syndrome is related to abnormal translation caused by defects in RNAi-related pathways. In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

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

Application Methods: Western Blotting

Background: Glucose-6-phosphate dehydrogenase (G6PD) catalyses the first, and rate-limiting, step of the pentose phosphate pathway (1). The NADPH generated from this reaction is essential to protect cells from oxidative stress (1). Research studies have shown that p53 interacts with G6PD and inhibits its activity, therefore suppressing glucose consumption through the pentose phosphate pathway (2). In cancer cells with p53 mutations, the increased glucose consumption is directed towards increased biosynthesis, which is critical for cancer cell proliferation (2).

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

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

Background: G9a, also known as Euchromatic histone-lysine N-methyltransferase 2 (EHMT2), is a member of a family of histone lysine methyltransferases, each of which contains a conserved catalytic SET domain originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins (1). Recombinant G9a can mono-, di- and tri-methylate histone H3 on Lys9 and Lys27 in vitro (1,2). However, in vivo G9a forms a complex with GLP, a G9a-related histone methyltransferase, and together these proteins function as the major euchromatic histone H3 Lys9 mono- and di-methyltransferases, creating transcriptionally repressive marks that facilitate gene silencing (3,4). G9a methylates itself on Lys165, a modification that regulates the association of HP1 repressor proteins with the G9a/GLP complex (5). The G9a/GLP complex also contains Wiz, a zinc finger protein that is required for G9a/GLP hetero-dimerization and complex stability (6). Wiz contains two CtBP co-repressor binding sites, which mediate the association of the G9a/GLP with the CtBP co-repressor complex (6). In addition, G9a and GLP are components of other large transcriptional co-repressor complexes, such as those involving E2F6 and CDP/cut (7-9). G9a interacts with DNMT1, and both proteins are required for methylation of DNA and histone H3 (Lys9) at replication foci, providing a functional link between histone H3 Lys9 and CpG methylation during DNA replication (10). G9a activity is critical for meiotic prophase progression, as mutant mice deficient in germ line G9a show a large loss of mature gametes (11). In addition, G9a facilitates increased global levels of di-methyl histone H3 (Lys9) during hypoxic stress and increased G9a expression is associated with hepatocelluar carcinoma (12,13).

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

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

Background: G9a, also known as Euchromatic histone-lysine N-methyltransferase 2 (EHMT2), is a member of a family of histone lysine methyltransferases, each of which contains a conserved catalytic SET domain originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins (1). Recombinant G9a can mono-, di- and tri-methylate histone H3 on Lys9 and Lys27 in vitro (1,2). However, in vivo G9a forms a complex with GLP, a G9a-related histone methyltransferase, and together these proteins function as the major euchromatic histone H3 Lys9 mono- and di-methyltransferases, creating transcriptionally repressive marks that facilitate gene silencing (3,4). G9a methylates itself on Lys165, a modification that regulates the association of HP1 repressor proteins with the G9a/GLP complex (5). The G9a/GLP complex also contains Wiz, a zinc finger protein that is required for G9a/GLP hetero-dimerization and complex stability (6). Wiz contains two CtBP co-repressor binding sites, which mediate the association of the G9a/GLP with the CtBP co-repressor complex (6). In addition, G9a and GLP are components of other large transcriptional co-repressor complexes, such as those involving E2F6 and CDP/cut (7-9). G9a interacts with DNMT1, and both proteins are required for methylation of DNA and histone H3 (Lys9) at replication foci, providing a functional link between histone H3 Lys9 and CpG methylation during DNA replication (10). G9a activity is critical for meiotic prophase progression, as mutant mice deficient in germ line G9a show a large loss of mature gametes (11). In addition, G9a facilitates increased global levels of di-methyl histone H3 (Lys9) during hypoxic stress and increased G9a expression is associated with hepatocelluar carcinoma (12,13).

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

Application Methods: Western Blotting

Background: The Grb-associated binder (Gab) family is a family of adaptor proteins recruited by a wide variety of receptor tyrosine kinases (RTKs) such as EGFR, HGFR, insulin receptor, cytokine receptor and B cell antigen receptors. Upon stimulation of RTKs by their cognate ligand, Gab is recruited to the plasma membrane where it is phosphorylated and functions as a scaffold (1-4). Multiple tyrosine phosphorylation sites of Gab1 protein have been identified (5). Phosphorylation of Tyr472 regulates its binding to p85 PI3 kinase (6,7). Phosphorylation of Gab1 at Tyr307, Tyr373 and Tyr407 modulates its association to PLCγ (8). Phosphorylation of Tyr627 and Tyr659 is required for Gab1 binding to and activation of the protein tyrosine phosphatase SHP2 (6,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: GABA (γ-aminobutyric acid) is the primary inhibitory neurotransmitter in the central nervous system and interacts with three different receptors: GABA(A), GABA(B) and GABA(C) receptor. The ionotropic GABA(A) and GABA(C) receptors are ligand-gated ion channels that produce fast inhibitory synaptic transmission. In contrast, the metabotropic GABA(B) receptor is coupled to G proteins that modulate slow inhibitory synaptic transmission (1). Functional GABA(B) receptors form heterodimers of GABA(B)R1 and GABA(B)R2 where GABA(B)R1 binds the ligand and GABA(B)R2 is the primary G protein contact site (2). Two isoforms of GABA(B)R1 have been cloned: GABA(B)R1a is a 130 kD protein and GABA(B)R1b is a 95 kD protein (3). G proteins subsequently inhibit adenyl cylase activity and modulate inositol phospholipid hydrolysis. GABA(B) receptors have both pre- and postsynaptic inhibitions: presynaptic GABA(B) receptors inhibit neurotransmitter release through suppression of high threshold calcium channels, while postsynaptic GABA(B) receptors inhibit through coupled activation of inwardly rectifying potassium channels. In addition to synaptic inhibition, GABA(B) receptors may also be involved in hippocampal long-term potentiation, slow wave sleep and muscle relaxation (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: GABAA receptor associated protein (GABARAP) is an Atg8 family protein with a key role in autophagy, which was originally discovered as a protein associated with the GABAA receptor regulating receptor trafficking to the plasma membrane (1). Proteins in this family, including microtubule-associated protein light chain 3 (LC3) and GATE-16 (GABARAPL2), become incorporated into the autophagosomal membranes following autophagic stimuli such as starvation (2). Like the other family members, GABARAP is cleaved at its carboxyl terminus, which leads to conjugation by either of the phospholipids phosphatidylethanolamine or phosphatidylserine (3,4). This processing converts GABARAP from a type I to a type II membrane bound form involved in autophagosome biogenesis. Processing of GABARAP involves cleavage by Atg4 family members (5,6) followed by conjugation by the E1 and E2 like enzymes Atg7 and Atg3 (7,8). GABARAPL1/GEC1, a protein that is highly related to GABARAP, was identified as an estrogen inducible gene, and is also associated with autophagosomes (9-11).

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

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

Background: GABAA receptor associated protein (GABARAP) is an Atg8 family protein with a key role in autophagy, which was originally discovered as a protein associated with the GABAA receptor regulating receptor trafficking to the plasma membrane (1). Proteins in this family, including microtubule-associated protein light chain 3 (LC3) and GATE-16 (GABARAPL2), become incorporated into the autophagosomal membranes following autophagic stimuli such as starvation (2). Like the other family members, GABARAP is cleaved at its carboxyl terminus, which leads to conjugation by either of the phospholipids phosphatidylethanolamine or phosphatidylserine (3,4). This processing converts GABARAP from a type I to a type II membrane bound form involved in autophagosome biogenesis. Processing of GABARAP involves cleavage by Atg4 family members (5,6) followed by conjugation by the E1 and E2 like enzymes Atg7 and Atg3 (7,8). GABARAPL1/GEC1, a protein that is highly related to GABARAP, was identified as an estrogen inducible gene, and is also associated with autophagosomes (9-11).

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

Application Methods: Western Blotting

Background: GABAA receptor associated protein (GABARAP) is an Atg8 family protein with a key role in autophagy, which was originally discovered as a protein associated with the GABAA receptor regulating receptor trafficking to the plasma membrane (1). Proteins in this family, including microtubule-associated protein light chain 3 (LC3) and GATE-16 (GABARAPL2), become incorporated into the autophagosomal membranes following autophagic stimuli such as starvation (2). Like the other family members, GABARAP is cleaved at its carboxyl terminus, which leads to conjugation by either of the phospholipids phosphatidylethanolamine or phosphatidylserine (3,4). This processing converts GABARAP from a type I to a type II membrane bound form involved in autophagosome biogenesis. Processing of GABARAP involves cleavage by Atg4 family members (5,6) followed by conjugation by the E1 and E2 like enzymes Atg7 and Atg3 (7,8). GABARAPL1/GEC1, a protein that is highly related to GABARAP, was identified as an estrogen inducible gene, and is also associated with autophagosomes (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunofluorescence (Frozen)

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

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

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

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

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

Application Methods: Western Blotting

Background: GADD45 α, β and γ are an evolutionarily conserved, homologous family of nuclear proteins that function as stress sensors for cellular physiological and environmental damage. GADD45 proteins are required for the activation of the G2/M checkpoint induced by UV radiation or alkylating agents (1). GADD45-induced G2/M checkpoint is regulated through inactivation of Cdc2-cyclin B1 kinase (2). GADD45 forms a complex with p21 and Cdc2, and may serve as core for interaction with other cell cycle regulators (3,4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Galectins are a family of β-galactose binding proteins that are characterized by an affinity for poly-N-acetyllactosamine-enriched glycoconjugates and a carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T-cell apoptosis (6), and immune responses (7).Galectin-3/LGALS3 is involved in several diverse biological functions. Galectin-3/LGALS3 binds IgE (8). Galectin-3/LGALS3 is an unusual protein in that can be found both extracellularly and intracellularly. Intracellularly, galectin-3/LGALS3 can localize to the cytoplasm, nucleus, or both, depending on cell type and experimental conditions. Nuclear galectin-3/LGALS3 has been identified as a pre-mRNA splicing factor (9). Galectin-3/LGALS3 production has been shown to increase during inflammation and in obesity, and the protein itself can have an inflammatory effect under certain conditions (10). Galectin-3/LGALS3 forms a complex with α3, β1 integrin to act as a surface receptor on endothelial cells for the NG2 proteoglycan, which triggers cell motility and angiogenesis (11). In addition to these functions, galectin-3/LGALS3 is also a required factor for the terminal differentiation of epithelial cells (12).