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Description:   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.
Catalog Number: 10075-516
Supplier: Prosci



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Description:   NCAM, as a member of the immunoglobulin superfamily of adhesion molecules is characterized by several immunoglobulin (Ig)-like domains. The extracellular part of NCAM consists of five of these Ig domains and two fibronectin type III homology regions. NCAM is encoded by a single copy gene composed of 26 exons. However, at least 20-30 distinct isoforms can be generated by alternative splicing and by posttranslational modifications, such as sialylation. During sialylation, polysialic acid (PSA) carbohydrates are attached to the extracellular part of NCAM. Through its extracellular region, NCAM mediates homophilic interactions. In addition, NCAM can also undergo heterophilic interactions by binding extracellular matrix components, such as laminin, or other cell adhesion molecules, such as integrins. NCAM is expressed on most neuroectodermal derived cell lines, tissues and neoplasm such as retinoblastoma, medulloblastoma, astrocytomas and neuroblastoma.
Catalog Number: 89360-750
Supplier: Genetex



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Description:   Irisin: Contrary to mouse, may not be involved in the beneficial effects of muscular exercise, nor in the induction of browning of human white adipose tissue.
Catalog Number: 10485-620
Supplier: Bioss



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Description:   Human serum albumin (HSA), the most abundant protein in human blood plasma, is essential for maintaining osmotic pressure. It is produced in the liver, consists of a single polypeptide chain, with 585 amino acids with 17 tyrosil residues and one tryptophan located in position 214. HSA is organized in three domains, I, II and III, each consisting of two subdomains, A and B. In the physiological states, HSA occurs in two forms – the non-modified HSA with a free thiol group of Cys-34, and the modified (oxidized) form (oHSA), also called human mercaptoalbumin (HMA) and human nonmercaptoalbumin (HNA), respectively. HMA and HNA are in equilibrium, depending on the redox state of Cys-34, and their ratio also varies depending on age and the diseased state. HSA functions primarily as a carrier protein for drugs, steroids, fatty acids, and thyroid hormones, and plays a role in stabilizing extracellular fluid volume.
Catalog Number: 75791-942
Supplier: Prosci



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Description:   The diffusible free radical gas nitric oxide (NO) affects a variety of physiological functions, and is a key regulator of the cardiovascular, nervous, and immune systems. NO is synthesized in many tissues from L-arginine, oxygen, and NADPH by three known isoforms of a heme-containing flavoprotein termed NO synthase (nNOS/NOS-I, iNOS/NOS-II, and eNOS/NOS-III). nNOS is a constitutively expressed neuronal NOS isoform that exits in its latent form until it is activated by the binding of calmodulin follo wing elevation of intracellular calcium levels. The C-terminus of nNOS contains a conserved serine residue, Ser1417, analogous to Ser1177 of the constitutively expressed endothelial NOS isoform (eNOS). Phosphorylation of Ser1417 is believed to regulate nNOS activation, particularly in glucose-sensing neurons, where inhibition of AMPK pathways by glucose and leptin serve to suppress nNOS activity, whereas activation of AMPK by insulin leads to nNOS activation.
Catalog Number: 95046-000
Supplier: Enzo Life Sciences



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Description:   Secondary Rabbit Anti-IgM mu chain Reacts with Sheep (Ovine)
Catalog Number: RL113-4107
Supplier: Rockland Immunochemical



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Description:   Secondary Chicken Anti-IgG (H&L) Reacts with Rat
Catalog Number: RL612-9102
Supplier: Rockland Immunochemical



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Description:   This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.
Catalog Number: 75895-802
Supplier: Biotium



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Description:   The 50 kDa type III intermediate filament protein glial fibrillary acidic protein (GFAP) is a major structural component of astrocytes. GFAP associates with the calcium binding protein annexin II-p2 and S-100. Association with these proteins together with phosphorylation regulates GFAP polymerization. Astroycytes respond to brain injury by proliferatin (astrogliosis), and one of the first events to occur during astrocyte proiliferation is increased GFAP expression. Interestingly, antibodies to GFAP have been detected in individuals with dementia. Anti-GFAP is ideal for investigators involved in Neuroscience Research, including Alexander Disease, Oligodendroglioma, Cytoskleton Remolding Neurofilaments and PIP3/AKT Signaling.
Catalog Number: 10801-598
Supplier: Rockland Immunochemical



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Description:   Secondary Sheep Anti-IgG (H&L) Reacts with Rat
Catalog Number: RL612-6102
Supplier: Rockland Immunochemical



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Description:   Matrix Metalloproteinase-1 (MMP-1) is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 contains several distinct domains: a prodomain that is cleaved upon activation, a catalytic domain containing the zinc binding site, a short hinge region, and a carboxyl terminal (hemopexin like) domain. MMP-1 can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL1, IGFBP3, IGFBP5, pro-MMP2, and pro-MMP9. A significant role of MMP1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into 3/4, 1/4 fragments. MMP1 may also be involved in enzyme cascades, cytokine regulation and cell surface molecule modulation.
Catalog Number: 75789-364
Supplier: Prosci



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Description:   In human liver cytosolic fractions, four forms of biliverdin reductase have been identified, including two biliverdin-IX Beta reductases and two biliverdin-IX Alpha reductases, designated isozymes I and II and isozymes III and IV, respectively. Biliverdin reductase A (BLVRA), also designated biliverdin-IX Alpha-reductase, belongs to the GFO/iIDH/MocA family and the biliverdin reductase subfamily. The gene that encodes this cytoplasmic protein maps to chromosome 7p14-cen. BLVRA reduces biliverdin IX ?(the ?methene bridge of the open tetrapyrrole) to bilirubin with the concomitant oxidation of an NADH or NADPH cofactor (bilirubin + NADP+ = biliverdin + NADPH). BLVRA is expressed primarily in liver.
Catalog Number: 10284-630
Supplier: Bioss



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Description:   In human liver cytosolic fractions, four forms of biliverdin reductase have been identified, including two biliverdin-IX Beta reductases and two biliverdin-IX Alpha reductases, designated isozymes I and II and isozymes III and IV, respectively. Biliverdin reductase A (BLVRA), also designated biliverdin-IX Alpha-reductase, belongs to the GFO/iIDH/MocA family and the biliverdin reductase subfamily. The gene that encodes this cytoplasmic protein maps to chromosome 7p14-cen. BLVRA reduces biliverdin IX ?(the ?methene bridge of the open tetrapyrrole) to bilirubin with the concomitant oxidation of an NADH or NADPH cofactor (bilirubin + NADP+ = biliverdin + NADPH). BLVRA is expressed primarily in liver.
Catalog Number: 10287-550
Supplier: Bioss



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Description:   Neuronal migration of the central nervous system is a specialized form of cell motility that takes place in the laminar structure of the cortical regions of brain. Astrotactin is a neuronal cell surface protein expressed on postmitotic neuronal precursors in the cerebellum, hippocampus, cerebrum, and olfactory bulb. Astrotactin 2 is a paralog of Astrotactin. Astrotactin mediates neuron-astroglial interactions and is also implicated in synaptic development as well as many other neuronal activities. Astrotactin has three epidermal growth factor repeat domains and two fibronectin type III repeat domains. The human Astrotactin gene shows extensive homology to the mouse Astrotactin gene. Mutations in the Astrotactin gene are linked to neuronal migration defects in both species.
Catalog Number: 10247-640
Supplier: Bioss



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Description:   Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Catalog Number: 10246-968
Supplier: Bioss



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Description:   RIMS-binding proteins (RIM-BPs) serve as adaptors during vesicle fusion and release by forming links between synaptic-vesicle fusion apparatuses and calcium channels. Specifically, RIM-BP2 (RIMS binding protein 2), also known as RBP2, is a 1,052 amino acid protein that links L-type Ca++ CP Alpha1D, N-type Ca++ CP Alpha1B, Rim1 and Rim2 during synaptic transmission. RIM-BP2 contains three fibronectin type-III domains and three SH3 domains, which are used to mediate binding to a proline-rich motifs. Existing as three alternatively spliced isoforms, RIM-BP2 is encoded by a gene that maps to human chromosome 12q24.33 and mouse chromosome 5 G1.3.
Catalog Number: 10256-570
Supplier: Bioss



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