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Product listing: IFN-β1 (D1D7G) Rabbit mAb, UniProt ID P01574 #73671 to Jak/Stat Pathway Inhibitors Antibody Sampler Kit, UniProt ID O14508 #8343

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Netrin proteins belong to an evolutionarily conserved family of laminin-like molecules that are involved in axon guidance and vascular development. These secreted proteins can have opposing functions depending on specific receptor association. For example, deleted in colorectal cancer (DCC) family receptors typically mediate cellular attraction (1,2) while netrin bound to UNC5 family receptors induce cellular repulsion (2-4). The uncoordinated 5B homolog (UNC5B) is a transmembrane protein with extracellular Ig-like domains and an intracellular region containing a protein-binding death domain and a putative DCC interaction domain (2). Homodimers composed of DCC receptor proteins mediate axonal attraction responses, while UNC5B homodimers and UNC5B-DCC heterodimers promote cellular repulsion (2). The netrin receptor UNC5B mediates apoptosis in the absence of netrin through the activation of DAP kinase (5) and is involved in leukocyte migration inhibition (6). Expression of UNC5B correlates with bladder cancer stage and the receptor is a potential predictor of both bladder and colorectal cancer prognosis and possible disease recurrence (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Lipocalin 2 (LCN2), also known as neutrophil gelatinase-associated lipocalin (NGAL), belongs to the lipocalin family. Proteins in this family exhibit considerable sequence diversity, but share a highly conserved structure composed of an eight-stranded antiparallel beta-barrel that encloses an internal ligand-binding site (1,2). LCN2 is considered as an iron transporter. LCN2 can bind bacterial siderophores and inhibits bacterial growth by iron depletion (3). It can also bind endogenous compounds like catechol in complex with iron (4). LCN2 was originally identified in neutrophils, and its expression was induced in many other tissues like kidney and liver in response to various pathologic states, such as infection, ischemia, and acute kidney injury. LCN2 is considered a biomarker for conditions like ischemic stroke, acute kidney injury, inflammatory and metabolic diseases (5-7).

$122
20 µl
$303
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

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

Background: Angiomotin (AMOT) is a widely expressed cell junction protein initially identified through its ability to bind angiostatin. Alternative splicing results in two isoforms of angiomotin, the full-length p130 and the amino-terminally truncated p80. These isoforms, along with angiomotin-like 1 (AmotL1) and angiomotin-like 2 (AmotL2) comprise the Motin protein family. Angiomotin is important in endothelial cell polarity, migration and blood vessel formation during development, as well as in signaling through small GTPases and the Hippo/YAP pathway (reviewed in 1).Research studies have shown that angiomotin expression regulates migration and proliferation of breast cancer cells (2,3).

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

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: SV2s are a family of synaptic vesicle proteins expressed in both neurons and endocrine cells. SV2s function in the regulation of synaptic vesicle traffic, cytoplasmic Ca2+ levels in the nerve terminal during repetitive stimulation and the facilitation of synaptic transmission. There are three isoforms of SV2: SV2A, SV2B and SV2C. Each of these isoforms are structured similarly but expressed varyingly. SV2C, a minor isoform of SV2, expressed in a small subset of neurons located within the basal forebrain, midbrain and brainstem. SV2B, a major isoform of SV2 is expressed more abundantly, although rarely without the coexpression of SV2A. SV2A, the other major isoform of SV2 is the most widely expressed. SV2A is located in the presynaptic nerve terminals of almost every neuron throughout the nervous system. In addition, it is also located in most neuroendocrine secretory granules (1). SV2A has been identified as a critical protein for proper function of the central nervous system and has been linked to the physiopathology of epilepsy (2). In addition to the epileptic affects of this protein, mutations in it have also been seen to result in schizophrenia (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: SPARC (secreted protein acidic and rich in cysteine), also known as osteonectin and BM40, is a secreted matricellular glycoprotein that belongs to a group of functionally related glycoproteins that includes tenascins C and X, thrombospondins 1 and 2, and osteopontin (1). Members in this class of glycoproteins are involved in tissue renewal, tissue remodeling, and embryonic development and work by exerting counter-adhesive and antiproliferative effects that lead to changes in cell shape, disruption of cell adhesion, and inhibition of the cell cycle (2). SPARC is expressed at high levels in bone tissue but is widely distributed in many other tissues and cell types (3), and is known to be associated with tissues undergoing morphogenesis, angiogenesis, mineralization, and other pathological responses to injury and tumorigenesis (4,5). SPARC has also been linked with obesity and diabetes (6).

$262
3 nmol
300 µl
SignalSilence® Stat3 siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Stat3 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Mouse

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: Rab11 family proteins consist of closely related Rab11a, Rab11b, and Rab25. They are small GTPases thought to play an essential role in regulating endocytic membrane traffic (1,2). The GTP-bound active state Rab11 proteins interact with the Rab11 family interacting proteins (Rab11FIPs) via a conserved carboxy-terminal Rab11-binding domain (3,4). At least six members of the Rab11FIPs have been identified. Based on sequence homology and domain structures, Rab11FIP1, Rab11FIP2 and Rab11FIP5 are categorized as class I subfamily members, whereas Rab11FIP3 and Rab11FIP4 belong to the class II subfamily that bind Arf6 and Rab11 proteins (5-7). Research studies have implicated Rab11 family proteins and their interacting effectors in carcinogenesis (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: NCK1 (also known as NCK or NCKα) is a broadly expressed oncogenic adapter protein consisting of three SH3 domains and one SH2 domain (1-3). NCK1 becomes phosphorylated upon activation of variety of cell surface receptors and is involved in actin cytoskeletal organization induced by many stimuli (4-6). NCK2 (also known as NCKβ), a homolog of NCK1, has an overlapping expression pattern and redundant functions with NCK1 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 55 kDa centrosomal protein (CEP55) is a widely expressed centrosome and midbody-associated protein that regulates cytokinesis, including completion of the final step during cytokinesis known as abscission (1,2). CEP55 activity during abscission is negatively regulated by p53 through Polo-like kinase 1 (3,4). The breast and ovarian cancer DNA repair protein BRCA2 interacts with CEP55 and plays a regulatory role during abscission (5). Research studies demonstrate that CEP55 is also involved in the regulation of Akt signaling, autophagy, and may be a biomarker in human cancer (reviewed in 6). The correlated overexpression of CEP55, the transcription factor FoxM1, and the HELLS helicase is seen in head and neck squamous cell carcinoma (7,8). Additional studies demonstrate that CEP55 expression regulates cell proliferation in gastric carcinoma (9).

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

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

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

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: SET7/SET9 is a member of the SET domain-containing family, and can specifically methylate Lys4 on histone H3 (1). Like most other lysine-directed histone methyltransferases, it contains a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste and Trithorax proteins. Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Methylation of histone H3 Lys4 enhances transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (4,5). In addition, methylation of lysine 4 blocks transcriptional repression by inhibiting the binding of the NURD histone deacetylation complex to the amino-terminal tail of histone H3 and interfering with SUV39H1-mediated methylation of histone H3 Lys9 (1). SET7/SET9 is highly active on free histone H3, but only very weakly methylates H3 within nucleosomes (1). Besides histones, SET7/SET9 also methylates Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein (6,7). Methylation of TAF10 stimulates transcription in a promoter-specific manner by increasing the affinity of TAF10 for RNA polymerase II, which may potentiate pre-initiation complex formation (6). Methylation of p53 at Lys372 increases protein stability and leads to upregulation of target genes such as p21. Thus the loss of SET7/SET9 may represent another mechanism for the inactivation of p53 in human cancers (7).

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

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

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1,2). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Research studies have shown that common variants of the human liver fatty acid binding protein gene FABP1 play a role in the development of type 2 diabetes and insulin resistance (3).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-amylase catalyzes the cleavage of 1, 4-α-D-glucosidic bonds in oligosaccharides and polysaccharides (1). The enzyme is normally produced and secreted in salivary glands (salivary α-amylase or AMY1) and pancreas (pancreatic α-amylase or AMY2A) (1). Studies reported the release of an ectopically expressed α-amylase in certain tumors (1). Furthermore, a new type of α-amylase (carcinoid α-amylase or AMY2B) was identified in a lung carcinoid tissue (2-4). The ectopic expression of α-amylase in a neuroendocrine tumor was also reported (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Oct-4 (POU5F1) is a transcription factor highly expressed in undifferentiated embryonic stem cells and embryonic germ cells (1). A network of key factors that includes Oct-4, Nanog, and Sox2 is necessary for the maintenance of pluripotent potential, and downregulation of Oct-4 has been shown to trigger cell differentiation (2,3). Research studies have demonstrated that Oct-4 is a useful germ cell tumor marker (4). Oct-4 exists as two splice variants, Oct-4A and Oct-4B (5). Recent studies have suggested that the Oct-4A isoform has the ability to confer and sustain pluripotency, while Oct-4B may exist in some somatic, non-pluripotent cells (6,7).

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

Application Methods: Western Blotting

Background: Apoptotic protease activating factor 1 (Apaf-1), originally identified as the mammalian homolog of the C. elegans apoptotic regulatory protein CED-4, is an important signaling protein involved in the activation of caspase-9 during apoptosis (1). Cytosolic Apaf-1 forms a complex with caspase-9 in the presence of cytochrome c and dATP, ultimately leading to caspase-9 activation and subsequent activation of caspase-3 (2,3). The protein contains an amino-terminal CARD domain, a central CED-4 homology domain, and multiple WD-40 repeats at the carboxy-terminus. Several isoforms of Apaf-1 are expressed through alternative splicing generating a small insert following the CARD domain as well as an extra WD-40 repeat (4). Apaf-1 knock-out mice display widespread defects in apoptosis and resistance to a variety of apoptotic stimuli (5,6).

$178
100 µl
APPLICATIONS

Application Methods: Western Blotting

The Resazurin Cell Viability Kit is a fluorescent assay that detects cellular metabolic activity. The blue nonfluorescent resazurin reagent is reduced to highly fluorescent resorufin by dehydrogenase enzymes in metabolically active cells. This conversion only occurs in viable cells and thus, the amount of resorufin produced is proportional to the number of viable cells in the sample. The resorufin formed in the assay can be quantified by measuring the relative fluorescence units (RFU) using a fluorometer (Ex=530-570 nm, Em=590-620 nm).
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

The Autophagy Vesicle Nucleation Antibody Sampler Kit provides an economical means of detecting target proteins involved in autophagosome formation and maturation. The kit contains enough antibody to perform two western blot experiments per primary antibody.
$489
96 assays
1 Kit
The PathScan® Phospho-Acetyl-CoA Carboxylase (Ser79) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of acetyl-CoA carboxylase (ACC) when phosphorylated at Ser79. A phospho-ACC (Ser79) rabbit antibody has been coated onto the microwells. After incubation with cell lysates, phospho-ACC protein is captured by the coated antibody. Following extensive washing, an ACC mouse detection mAb is added to detect the captured ACC protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of ACC phosphorylated at Ser79.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$489
96 assays
1 Kit
CST's PathScan® Total Akt1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Akt1 protein. An Akt Antibody has been coated onto the microwells. After incubation with cell lysates, the Akt protein is captured by the coated antibody. Following extensive washing, Akt1 Mouse Monoclonal Antibody is added to detect the captured total Akt1 protein. Anti-Mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total Akt1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

The AMPK Subunit Antibody Sampler Kit provides an economical means to investigate the role played by all AMPK subunits in cellular energy homeostasis. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.

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).

$489
96 assays
1 Kit
CST's PathScan® Phospho-IGF-I Receptor beta (Tyr1131) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of IGF-I receptor beta protein when phosphorylated at Tyr1131. A Phospho-IGF-I Receptor beta (Tyr1131) Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, phospho-IGF-I Receptor beta is captured by the coated antibody. Following extensive washing, an IGF-I Receptor Mouse Antibody is added to detect the captured phospho-IGF-I receptor protein. Anti-mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for this developed color is proportional to the quantity of IGF-I receptor protein phosphorylated at Tyr1131.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

The Jak/Stat Pathway Inhibitors Antibody Sampler Kit provides an economical means to examine several inhibitors of Jak/Stat signaling, including PIAS1, PIAS3, PIAS4, SOCS1, SOCS2, and SOCS3. The kit contains enough primary antibody to perform two western blot experiments with each primary antibody.