"Test Lead"

Supplier: Prosci

Following activation by double-stranded RNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the translation initiation factor EIF2S1, which leads to an inhibition of the initiation of protein synthesis. Double-stranded RNA is generated during the course of a viral infection.

Supplier: Genetex

The protein encoded by this gene is similar to an iron transport protein found in mouse. The mouse protein is similar to ceruloplasmin, a serum multi-copper ferroxidase, and is thought to be a membrane-bound protein responsible for transport of dietary iron from epithelial cells of the intestinal lumen into the circulatory system. In mouse, defects in this gene can lead to severe microcytic anemia. Three transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq]

Supplier: Genetex

CD95, also known as FAS or APO-1, is a 36 kDa cell surface type I- membrane glycoprotein with an apparent molecular weight of 44 kDa on SDS-PAGE. CD95 is a member of the TNF receptor family, which includes TNFR-1, TNFR-2, CD27, CD30 and CD40. Binding of CD95 Ligand to CD95 or crosslinking of CD95 by anti-CD95 monoclonal antibodies leads to apoptosis of CD95 expressing cells. CD95 belongs to a subgroup of family members that have a death domain (DD) which contains 70 amino acids near the carboxyl-terminal region of the molecule. The binding of adaptor molecules to this DD is responsible for transmitting the death signal for apoptosis. Stimulation of CD95 results in aggregation of its DD, leading to the recruitment of FADD and caspase-8 that together with the receptor form the death-inducing signaling complex (DISC).

Supplier: Prosci

ATG101 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein ATG1. ATG101 is a recently discovered protein that stabilizes ATG13, another autophagy protein that forms a complex with the mammalian homologs of ATG1, ULK1 and ULK2, and with FIP200. This complex is a target of TOR phosphorylation under normal conditions; inhibition of TOR by rapamycin or leucine deprivation leads to dephosphorylation of ATG13, ULK1 and ULK2, which then leads to autophagy. ATG101 also interacts with ULK1 and is essential for autophagy.

Supplier: Southern Biotechnology

CD3, a member of the immunoglobulin superfamily of cell surface receptors, is comprised of five invariable chains ranging from 16-28 kDa and is closely associated with the T cell antigen receptor (TCR). CD3 is expressed on 70-80% of normal peripheral blood lymphocytes and on 10-20% of thymocytes. It plays a major role in signaling during antigen recognition, leading to T cell activation. The monoclonal antibody UCHT1 reacts with the 20 kDa ε chain of the CD3/TCR complex.

Supplier: Prosci

Following activation by double-stranded RNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the translation initiation factor EIF2S1, which leads to an inhibition of the initiation of protein synthesis. Double-stranded RNA is generated during the course of a viral infection.

Supplier: Genetex

Human interleukin 2 (IL2) is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

Supplier: Rockland Immunochemical

Variable Lipoprotein Surface-Exposed protein, or VlsE, is a lipoprotein on the surface of the Lyme Disease spirochete Borrelia burgdorferi, detectable during all its life stages. VlsE has variable regions (VRs) and invariable regions (IRs). Some IRs are anchored in the outer membrane of the bacteria and some are antigens exposed on the membrane surface. Replacement of the VR by Borrelia within days of being transferred to a mammalian host presents new surface antigens to the host immune system, and helps Borrelia avoid a strong reaction by host immune systems. The VlsE is apparently not modified as much in the tick or in the rodent vector, when compared to in the mammal host. Several putative envelope proteins of B. burgdorferi appear to be expressed only in the infected mammalian host. The VRs are antigenic, irregularly shaped loops on the bacterial surface which may help to hide both membrane-incorporated and surface portions of adjacent proteins from immune cells. These VR loops are coded by antigenic cassettes. The protein loops can therefore be switched in or out of the protein, or different type loops traded. In B. burgdorferi there seem to be at least fifteen different VlsE cassettes that can insert into any of the variable regions of VlsE, allowing it to appear as millions of different antigens. Similar, but smaller, systems also operate for OSP-A, OSP-B, OSP-C, and other proteins. One IR region, C6, of the VlsE protein, consistently stimulates a strong immune response. Its presentation may be a decoy that misdirects the immune system from less protected sites by causing competion for binding antibodies. The bound antibodies are thus not available for binding important therapeutic proteins. This may help Borrelia to enter T-cells, leading to their destruction. Because IR6 is invariable and found in all life stages of B. burgdorferi, it has been used in an ELISA diagnostic test for early IgM of Lyme Disease.

Supplier: Genetex

Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.

Supplier: Genetex

After binding Acetylcholine, the Nicotinic Acetylcholine Receptor (AChR) responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different type of subunits: alpha and beta. This antibody binds to native subunits as well as denatured subunits although with lower affinity. Clone 270 is useful for immunoisolating and pharmacologically characterizing AChRs, immunopurification of AChRs, and is also useful histologically.

Supplier: Prosci

Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

Supplier: Genetex

Integrin beta 1, also known as CD29, is a 130 kDa transmembrane glycoprotein that forms noncovalent complexes with various Integrin alpha subunits (including alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, and alpha 6, also known as CD49a, CD49b, CD49c, CD49d, CD49e, and CD49f, respectively) to form the functional receptors that bind to specific extracellular matrix proteins. Integrin receptors are involved in the regulation of a variety of important biological functions, including embryonic development, wound repair, hemostasis, and prevention of programmed cell death. They are also implicated in abnormal pathological states such as tumor directed angiogenesis, tumor cell growth, and metastasis. These heterodimeric receptors bridge the cytoplasmic actin cytoskeleton with proteins present in the extracellular matrix and/or on adjacent cells. The clustering of integrins on a cell surface leads to the formation of focal contacts. Interactions between integrins and the extracellular matrix lead to activation of signal transduction pathways and regulation of gene expression.

Supplier: Prosci

RCAN1 interacts with calcineurin A and inhibits calcineurin-dependent signaling pathways, possibly affecting central nervous system development. This gene is located in the minimal candidate region for the Down syndrome phenotype, and is overexpressed in the brain of Down syndrome fetuses. Chronic overexpression of this gene may lead to neurofibrillary tangles such as those associated with Alzheimer disease.The protein encoded by this gene interacts with calcineurin A and inhibits calcineurin-dependent signaling pathways, possibly affecting central nervous system development. This gene is located in the minimal candidate region for the Down syndrome phenotype, and is overexpressed in the brain of Down syndrome fetuses. Chronic overexpression of this gene may lead to neurofibrillary tangles such as those associated with Alzheimer disease. Three transcript variants encoding three different isoforms have been found for this gene.

Supplier: Genetex

The protein encoded by this gene is a type I integral membrane protein localized in the intermediate region between the endoplasmic reticulum and the Golgi, presumably recycling between the two compartments. The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of animal cells. Mutations in the gene are associated with a coagulation defect. Using positional cloning, the gene was identified as the disease gene leading to combined factor V-factor VIII deficiency, a rare, autosomal recessive disorder in which both coagulation factors V and VIII are diminished. [provided by RefSeq]

Supplier: Prosci

Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

Supplier: Prosci

Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.