Wyszukano: DISCOVER+ECHO

Numer katalogowy: (PRSI3315)

Producent: ProSci Inc.

Opis: NAIP Antibody: Neuronal apoptosis inhibitor protein (NAIP) was the first human inhibitor of apoptosis protein (IAP) identified and was discovered by its association with the neurodegenerative disorder spinal muscular atrophy. Members of the IAP family contain one to three copies of an approximately 70 amino acid motif termed baculovirus IAP repeat (BIR); these BIRs promote protein-protein interactions with various caspases such as caspase-3, -7, and -9 as well as members of the TRAF family of signal molecules. Unlike other IAPs however, NAIP requires ATP to bind caspase-9 and is not inhibited by the IAP-inhibiting molecule Smac/DIABLO, suggesting that NAIP is unique among the IAPs in its regulation of its activity. Finally, although only one human NAIP protein has been identified, other shorter NAIP mRNA transcripts have been reported.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI3797)

Producent: ProSci Inc.

Opis: IL-27 Antibody: Like interleukin-23 (IL-23), IL-27 is a recently discovered member of the IL-6/IL-12 family of proinflammatory and immunoregulatory cytokines. It exists as a heterodimer composed of the p40-related protein EBI3 and an IL-12 p35-related protein termed p28. IL-27 is produced after activation by antigen-presenting cells and induces proliferation of naïve but not memory CD4+ T-cells. It acts by binding to its receptor WSX-1 and gp130 which results in the activation of a Jak/STAT signaling cascade, suggesting the IL-27 is involved in the regulation of immune processes. It has been suggested that IL-27 can also be used as a therapeutic agent against cancer as it can also induce tumor-specific anti-tumor activity mediated through CD8+ T-cells, IFN-gamma, and T-bet.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI4675)

Producent: ProSci Inc.

Opis: BICD2 Antibody: BICD2 is the second human homolog discovered to the Drosophila Bicaudal-D protein that forms part of the cytoskeleton and mediates the correct sorting of mRNAs for oocyte- and axis-determining factors during oogenesis. Similar to the highly homologous protein BICD1, BICD2 can bind to dynein-dynactin complex, primarily through the dynamitin subunit of dynactin. The C-terminus of BICD2 targets the protein to the Golgi complex while the N-terminal domain of BICD2 co-immunoprecipitates with cytoplasmic dynein, suggesting BICD2 plays a role in the dynein-dynactin interaction on the surface of membranous organelles. Mice engineered to overexpress the BICD2 amino terminal domain in neurons developed amyotrophic lateral sclerosis (ALS)-like features such as Golgi fragmentation, neurofilament swelling in proximal axons, etc., suggesting that impaired dynein/dynactin function may explain some of the pathological features observed in ALS patients.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI5405)

Producent: ProSci Inc.

Opis: SKA3 Antibody: Upon entry into mitosis, the cell's microtubule (MT) network forms the mitotic spindle, allowing the segregation of paired chromosomes. Proteinaceous structures on centromeric chromatin termed kinetochores (KT) are essential for the proper attachment of the chromosomes to the spindle MTs. A recently discovered spindle and kinetochore complex, comprised of proteins SKA1, SKA2, and SKA3, has been found to be required for stable KT-MT interactions and timely anaphase onset. Like with SKA1 or SKA2, depletion of SKA3 by siRNA delays anaphase transition, resulting in a prolonged a metaphase-like state. These SKA3-depleted cells accumulate high levels of the checkpoint protein Bub1 at kinetochores, suggesting the SKA complex plays a key role in spindle checkpoint silencing and the maintenance of chromosome cohesion in mitosis.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI5801)

Producent: ProSci Inc.

Opis: 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.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI3485)

Producent: ProSci Inc.

Opis: TOR Antibody: The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. It was initially discovered as a kinase whose ability to stimulate T cell proliferation in response to IL-2 could be inhibited by the immunosuppressive drug rapamycin. Rapamycin inhibits TOR in other cell types resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. TOR is normally associated with the regulatory proteins RAPTOR and GbetaL. Its downstream targets are thought to be the ribosomal protein S6 kinases and the eukaryotic initiation factor 4E binding proteins (4EBPs). Regulation of these protein families allows TOR to control protein biosynthesis.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI3633)

Producent: ProSci Inc.

Opis: PIST 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 and is negatively regulated by TOR (Target of rapamycin). PIST, a PDZ-containing protein, was discovered in a yeast two-hybrid system as a binding partner to Beclin-1, a Bcl-2-interacting protein homologous to the yeast autophagy gene apg6. Experiments with mutant PIST proteins lacking the PDZ domain showed that PIST interaction with Beclin-1 through its coiled-coil domain can modulate Beclin-1 activity and suggest that PIST interactions with other proteins through its PDZ domain may regulate the activity of PIST and Beclin-1.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI4687)

Producent: ProSci Inc.

Opis: CPEB1 Antibody: CPEB1 is an RNA binding protein that contains an RNA-recognition motif and a zinc finger-containing region found in a wide range of vertebrates and invertebrates. CPEB1 forms the nucleus of a complex of factors that regulate poly(A) elongation and promotes polyadenylation-induced translation. CPEB1 mediates many diverse biological processes such as germ cell development, cell division and senescence, and synaptic plasticity. Recently, it was discovered that CPEB1 is involved in beta-catenin mRNA translation and cell migration in astrocytes as well as regulating hypoxia-inducible factor (HIF)-1 expression, demonstrating the wide range of processes in which CPEB1 plays a role. At least four isoforms of CPEB1 are known to exist.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI32-155)

Producent: ProSci Inc.

Opis: Fibulin 5(FBLN5), with 448-amino acid protein (about 50 kDa), is a recently discovered multifunctional extracellular matrix protein that mediates endothelial cell adhesion through integrin ligation, regulates cell growth and motility in a context-specific manner, and prevents elastinopathy in vivo. Fibulin-5 is abundantly expressed in great vessels and cardiac valves during embryogenesis, and in many adult tissues including the aorta, lung, uterus and skin, all of which contain abundant elastic fibres. Decreased fibulin-5 may contribute to the pathogenesis of aortic dissection by impairing elastic fiber assembly. Fibulin-5 is also a good marker of skin ageing and that the earlier loss of fibulin-5 may involve age-dependent changes in other elastic fibre components.

j.m.: 1 * 100 µl

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Numer katalogowy: (BOSSBS-5855R-A750)

Producent: Bioss

Opis: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilisation. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.

j.m.: 1 * 100 µl

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Numer katalogowy: (PRSI90-492)

Producent: ProSci Inc.

Opis: Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumour cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.

j.m.: 1 * 10 µG

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Numer katalogowy: (PRSI5211)

Producent: ProSci Inc.

Opis: UCMA Antibody: UCMA is a secreted cartilage-specific protein that was discovered in a screen for differentially expressed genes in retinoic acid-treated mouse chondrocytes. It was also identified in a human chondrocyte EST screen for candidate genes of skeletal dysplasias. UCMA expression is thought to parallel that of collagen II with its expression decreasing with maturation chrondrocytes mature. UCMA is processed by a furin-like protease into two fragments, an amino-terminal fragment and a carboxy-terminal fragment (UCMA-C). Application of recombinant UCMA-C to primary osteoblasts, mesenchymal stem cells, and MC3T3-E1 pre-osteoblasts interferes with their osteogenic differentiation, but does not affect expression of chondrocyte-specific genes or chondrocyte proliferation, suggesting that UCMA may be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells. At least two isoforms of UCMA are known to exist.

j.m.: 1 * 100 µG

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Numer katalogowy: (PRSI4677)

Producent: ProSci Inc.

Opis: BICD2 Antibody: BICD2 is the second human homolog discovered to the Drosophila Bicaudal-D protein that forms part of the cytoskeleton and mediates the correct sorting of mRNAs for oocyte- and axis-determining factors during oogenesis. Similar to the highly homologous protein BICD1, BICD2 can bind to dynein-dynactin complex, primarily through the dynamitin subunit of dynactin. The C-terminus of BICD2 targets the protein to the Golgi complex while the N-terminal domain of BICD2 co-immunoprecipitates with cytoplasmic dynein, suggesting BICD2 plays a role in the dynein-dynactin interaction on the surface of membranous organelles. Mice engineered to overexpress the BICD2 amino terminal domain in neurons developed amyotrophic lateral sclerosis (ALS)-like features such as Golgi fragmentation, neurofilament swelling in proximal axons, etc., suggesting that impaired dynein/dynactin function may explain some of the pathological features observed in ALS patients.

j.m.: 1 * 100 µG

Wyprzedaż

Numer katalogowy: (PRSI3661)

Producent: ProSci Inc.

Opis: TRAF2 Antibody: Tumor necrosis factor (TNF) receptor associated factors (TRAFs) were initially discovered as adaptor proteins that link the TNF receptor superfamily to signaling pathways and are thus important regulators of cell death and cellular response to stress. TRAF proteins share a homology region that allows them to bind to cell receptors and other TRAF proteins, causing the activation of different signal cascades depending on the TRAFs involved. For example, TRAF2 and TRAF3 directly bind to the CD40, a TNF receptor superfamily member involved in inducing B cell immunity, and are critical for NF-kappa B activation in mouse B lymphocytes. TRAF2 along with TRAF6 has also been shown to be required for CD40 signaling in nonhemopoietic cells. TRAF2 also interacts with the TRFR superfamily member lymphotoxin-beta receptor (LTbetaR) in association with TRAF3 and the apoptosis inhibitors cIAP1 and Smac.

j.m.: 1 * 100 µG

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Numer katalogowy: (ROCK100-401-D60)

Producent: Rockland Immunochemicals

Opis: 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 10nm 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. Therefore, GFAP antibody is ideal for investigators involved in neuropathologic diseases and more generally in Neuroscience.

j.m.: 1 * 100 µl

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Numer katalogowy: (PRSI3039)

Producent: ProSci Inc.

Opis: AATF Antibody: AATF (apoptosis antagonizing transcription factor) was initially discovered as an interaction partner of ZIP kinase (ZIPK), a member of death-associated protein (DAP) kinase family of pro-apoptotic serine/threonine kinases. AATF is a phosphoprotein containing an acidic region and a putative leucine zipper domain and nuclear localization signal, features which are typical of transcription factors. AATF inhibits the ZIPK-mediated pro-apoptotic pathway and may activate other anti-apoptotic pathways. Recently, it has also been shown to protect neural cells against oxidative damage induced by amyloid b-peptide and to inhibit aberrant production of the beta-peptide by interacting with Par-4 (prostate apoptosis response-4), another pro-apoptotic leucine zipper protein that is associated with neuronal degeneration in Alzheimer's disease (AD), suggesting that AATF may have potential therapeutic applications in both familial and sporadic forms of AD.

j.m.: 1 * 100 µG

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