1082 Results for: "Test Lead"

Supplier: Prosci

B-raf Antibody: B-raf belongs to the raf/mil family of serine/threonine protein kinases and plays a role in regulating the MAP kinase/ERKs signaling pathway, which affects cell division, differentiation, and secretion. The Ras/Raf/MEK/ERK and Ras/PI3K/PTEN/Akt pathways interact with each other to regulate growth and in some cases tumorigenesis. Mutations in B-raf have been associated with several cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, and adenocarcinoma of lung, leading to speculation on the possibility of B-raf as a therapeutic target for treating cancers. Mutations in this gene have also been associated with cardiofaciocutaneous syndrome (CFCS), a disease characterized by heart defects, mental retardation and a distinctive facial appearance.

Supplier: Prosci

Glial Fibrillary Acidic Protein (GFAP) was discovered by Amico Bignami and co-workers as a major fibrous protein of multiple sclerosis plaques. It was subsequently found to be a member of the 10 nm or intermediate filament (IF) family, specifically the IF family Class III, which also includes peripherin, desmin and vimentin. GFAP is strongly and specifically expressed in astrocytes and certain other astroglia in the CNS, in satellite cells, peripheral ganglia, and in non-myelinating Schwann cells in peripheral nerves. In many damage and disease states GFAP expression is heavily upregulated in astrocytes. In addition, neural stem cells frequently strongly express GFAP. Point mutations in the protein coding region of the GFAP gene lead to Alexander disease which is characterized by the presence of abnormal astrocytes containing GFAP protein aggregates known as Rosenthal fibers.

Supplier: Prosci

ZC3H12A Antibody: ZC3H12A, also known as MCPIP, is an essential member of a family of novel CCCH-zinc finger proteins that regulate macrophage activation and may be involved in host immunity and inflammatory diseases. ZC3H12A has RNase activity that prevents some immune disorders by directly affecting the mRNA stability of interleukins such as IL-6 and IL12p40. Mice lacking the ZC3H12A gene suffered from severe anemia, and most dies within 12 weeks. Overexpression of ZC3H12A causes ER stress and induces a number of genes involved in apoptosis and autophagy, including JNK, PUMA, and beclin-1 in cardiac myoblasts, leading to cell death. ZC3H12A can also induce adipogenesis in 3T3-L1 pre-adipocytes in the absence of PPAPgamma, demonstrating the complex roles ZC3H12A plays.

Supplier: Genetex

In resting cells, NFkB is retained in the cytoplasm bound to inhibitory proteins of the IkB family. Degradation of IkB proteins occurs with cell activation, via of variety of signals, including inflammatory cytokines and bacterial lipopolysaccharides (LPS) as well as oxidative and fluid mechanical stress. This results in nuclear translocation of NFkB and the transcriptional gene activation of pro-inflammatory genes (1,9). NFkB plays a role in the development of numerous pathological states. Activation of NFkB induces gene programs leading to transcription of factors that promote inflammation, such as leukocyte adhesion molecules, cytokines, and chemokines. It is also thought that there are some substances with possible anti-inflammatory effects that are also NFkappaB regulated. There is some evidence indicating NFkB as a key factor in the pathophysiology of cardiac ischemia-reperfusion injury as well as the development of insulin dependent Diabetes Mellitus (3-4).

Supplier: Prosci

Interleukin 13 receptor, alpha 1 is also known as IL13RA1, NR4 and CD213A1 (cluster of differentiation 213A1), The IL13 R?1 cDNA encodes a 427 amino acid (aa) residue precursor protein with a putative 21 aa residue signal peptide, a 324 aa residue extracellular domain, a 23 aa residue transmembrane region and a 59 aa residue cytoplasmic tail. Human and mouseIL13R?1 share 76% aa sequence identity. IL13RA1 is a subunit of the interleukin 13 receptor. This subunit forms a receptor complex with IL4 receptor alpha, a subunit shared by IL13 and IL4 receptors. This subunit serves as a primary IL13-binding subunit of the IL13 receptor, and may also be a component of IL4 receptors. This protein has been shown to bind tyrosine kinase TYK2, and thus may mediate the signaling processes that lead to the activation of JAK1, STAT3 and STAT6 induced by IL13 and IL4.

Supplier: Prosci

B-raf Antibody: B-raf belongs to the raf/mil family of serine/threonine protein kinases and plays a role in regulating the MAP kinase/ERKs signaling pathway, which affects cell division, differentiation, and secretion. The Ras/Raf/MEK/ERK and Ras/PI3K/PTEN/Akt pathways interact with each other to regulate growth and in some cases tumorigenesis. Mutations in B-raf have been associated with several cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, and adenocarcinoma of lung, leading to speculation on the possibility of B-raf as a therapeutic target for treating cancers. Mutations in this gene have also been associated with cardiofaciocutaneous syndrome (CFCS), a disease characterized by heart defects, mental retardation and a distinctive facial appearance.

Supplier: Prosci

SOX4 is a member of the SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. It may act as a transcriptional regulator after forming a protein complex with other proteins, such as syndecan binding protein (syntenin). The protein may function in the apoptosis pathway leading to cell death as well as to tumorigenesis and may mediate downstream effects of parathyroid hormone (PTH) and PTH-related protein (PTHrP) in bone development. The solution structure has been resolved for the HMG-box of a similar mouse protein.This intronless gene encodes a member of the SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. The encoded protein may act as a transcriptional regulator after forming a protein complex with other proteins, such as syndecan binding protein (syntenin). The protein may function in the apoptosis pathway leading to cell death as well as to tumorigenesis and may mediate downstream effects of parathyroid hormone (PTH) and PTH-related protein (PTHrP) in bone development. The solution structure has been resolved for the HMG-box of a similar mouse protein. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Tonbo Biosciences

The RPA-T8 antibody is specific for the 32-34 kDa alpha chain of human CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor for antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Prosci

RWDD3 Antibody: RWDD3 (RSUME), a small RWD-containing protein, has a central role in sumoylation by enhancing SUMO conjugation in the regulatory network of immune-inflammatory signals. RWDD3 increases Ikappa Beta sumoylation and stability. In addition, RWDD3 inhibits TNF-alpha -induced kappaB-LUC (Luciferase) reporter activity, showing the functional consequence of Ikappa Beta increased stability. RSUME-enhanced sumoylation of Ikappa Beta leads to the inhibition of NF-kappa Beta activity on two well-known inflammatory genes, IL-8 and cyclooxygenase-2 (Cox-2) and therefore may also favor anti-inflammatory pathways. Expression of RWDD3 was induced under hypoxic conditions and it has a potential role during vascularization. Both BMP-4 and RWDD3 may be interesting targets for inhibiting steps involved in pituitary tumorigenesis.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Genetex

The transcription factor NFkB is widely recognized as a critical mediator of immune and inflammatory responses. In most cell types, NFkB is found in the cytoplasm where it is associated with an inhibitory protein known as IkB. An impressive variety of stimuli (tumor necrosis factor, interleukin 1, T-cell activation signals, bacterial endotoxins, viral transforming proteins, certain growth factors and reactive oxygen intermediates) lead to the rapid nuclear accumulation of NFkB by the induced phosphorylation and subsequent degradation of IkB. In the nucleus, NFkB regulates genes encoding cytokines, cytokine receptors, cell adhesion molecules, proteins involved in coagulation and genes involved in cell growth control. Additionally, NFkB is thought to be an important transcriptional regulator for HIV. Growing evidence indicates that the dysregulation of NFkB may be key to a number of diseases including arthritis and other inflammatory diseases, Alzheimer's disease, atherosclerosis and cancer.

Supplier: Prosci

APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by one of two beta-secretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the Alzheimer's disease patient's brains. Recently, Death Receptor 6 (DR6) was found to interact with an amino-terminal fragment of the Beta-amyloid protein (N-APP) in neurons, activating a caspase 6-dependent apoptotic event leading to axonal degeneration and pruning during development, suggesting that these two proteins are involved in neural development and may possibly play a role in Alzheimer's disease.

Supplier: Genetex

The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. At least eight alternatively spliced transcript variants encoding seven distinct isoforms have been described. The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform. [provided by RefSeq]

Supplier: Tonbo Biosciences

The RPA-T8 antibody is specific for the 32-34 kDa alpha chain of human CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor for antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Genetex

Enzymes of the cAMP-dependent phosphodiesterase type 4 (PDE4) family are important in hydrolyzing cAMP produced by G-protein coupled receptor (GPCR) stimulated adenylyl cyclases. In brain, more than 90% of cAMP formed by the stimulation of GPCRs is hydrolyzed by PDE4 enzymes. PDE4 enzymes are also important molecular targets for a variety of therapeutic agents like antidepressants, anti-asthmatics, and anti-inflammatory drugs. PDE4 family comprises 4 genes (PDE4A, B, C and D); each exhibiting multiple isozymes due to alternate splicing that leads to a larger number of distinct PDE4 variants. Members of the PDE4 family are regulated/activated by phosphorylation/dephosphorylation by cAMP-dependent protein kinase A and phosphatases. Protein-protein interactions and cellular trafficking of PDE4A enzymes play an important role in cAMP compartmentalization and cAMP-dependent signaling. In brain members of the PDE4A, B and D family are associated with GPCRs (adrenergic and dopaminergic) signaling.

Supplier: Prosci

Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Supplier: Prosci

MFNG is one of the evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. Western blots using two different antibodies against two unique regions of this protein target confirm the same apparent molecular weight in our tests.This gene is a member of the fringe gene family which also includes Radical and Lunatic fringe. They all encode evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta1,3 N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

MFNG is one of the evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. Western blots using two different antibodies against two unique regions of this protein target confirm the same apparent molecular weight in our tests.This gene is a member of the fringe gene family which also includes Radical and Lunatic fringe. They all encode evolutionarily conserved secreted proteins that act in the Notch receptor pathway to demarcate boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta1,3 N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Tonbo Biosciences

The 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor in antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: MOUSER ELECTRONICS MS

TEST LEADS MALE RED 2MM/4MM 3.9IN 10CM

Supplier: Prosci

GPVI Antibody: Glycoprotein VI (GP6) is a 58kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. It is uniquely expressed by cells of the megakaryocytic/platelet lineage, and is a member of the immunoglobulin gene superfamily, closely related to Fc receptor gamma chain (FcRgamma) and natural killer receptors. Glycoprotein VI plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcRgamma, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. GPVI deficiency can result in bleeding disorders. Further study should reveal the extent of GPVI involvement in thrombotic disease and allow the development of alternative anti-thrombotic compounds.

Supplier: Prosci

GPVI Antibody: Glycoprotein VI (GP6) is a 58kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. It is uniquely expressed by cells of the megakaryocytic/platelet lineage, and is a member of the immunoglobulin gene superfamily, closely related to Fc receptor gamma chain (FcRgamma) and natural killer receptors. Glycoprotein VI plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcRgamma, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. GPVI deficiency can result in bleeding disorders. Further study should reveal the extent of GPVI involvement in thrombotic disease and allow the development of alternative anti-thrombotic compounds.

Supplier: Prosci

APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by one of two beta-secretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the Alzheimer's disease patient's brains. Recently, Death Receptor 6 (DR6) was found to interact with an amino-terminal fragment of the beta-amyloid protein (N-APP) in neurons, activating a caspase 6-dependent apoptotic event leading to axonal degeneration and pruning during development, suggesting that these two proteins are involved in neural development and may possibly play a role in Alzheimer's disease.

Supplier: Genetex

Nuclear factor kappa B (NF-kB) is a ubiquitous transcription factor and an essential mediator of gene expression during activation of immune and inflammatory responses. NF-kB mediates the expression of a great variety of genes in response to extracellular stimuli. NF-kB is associated with IkB proteins in the cell cytoplasm, which inhibit NF-kB activity. Phosphorylation of I-kB by IkB kinase (IKK) complex leads to degradation of I-kB and activation of NF-kB. The IKK complex contains IKKa,IKKb, and IKKg. A novel IKK related kinase was recently identified and designated TBK1 (TANK-binding kinase 1), NAK (NF-kB-activating kinase), and T2K. NAK/TBK1 activates IKKb through direct phosphorylation. NAK/TBK1is activated by growth factors and PMA and mediates IKK and NF-kB activation in response to growth factors. NAK/TBK1 functions upstream of NIK and the IKK complex. NAK/TBK1 is also critical in protecting embryonic liver from apoptosis.

Supplier: MOUSER ELECTRONICS MS

TEST LEADS MALE BLACK 3.9IN 10CM 2MM/4MM

Supplier: Prosci

Interleukin 13 receptor, alpha 1 is also known as IL13RA1, NR4 and CD213A1 (cluster of differentiation 213A1), The IL13 R?1 cDNA encodes a 427 amino acid (aa) residue precursor protein with a putative 21 aa residue signal peptide, a 324 aa residue extracellular domain, a 23 aa residue transmembrane region and a 59 aa residue cytoplasmic tail. Human and mouseIL13R?1 share 76% aa sequence identity. IL13RA1 is a subunit of the interleukin 13 receptor. This subunit forms a receptor complex with IL4 receptor alpha, a subunit shared by IL13 and IL4 receptors. This subunit serves as a primary IL13-binding subunit of the IL13 receptor, and may also be a component of IL4 receptors. This protein has been shown to bind tyrosine kinase TYK2, and thus may mediate the signaling processes that lead to the activation of JAK1, STAT3 and STAT6 induced by IL13 and IL4.