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Catalog Number: (10781-998)
Supplier: Biosensis
Description: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).


Catalog Number: (10782-006)
Supplier: Biosensis
Description: FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons. SUBUNIT: Homodimer, associated by noncovalent forces. SUBCELLULAR LOCATION: Secreted protein. SIMILARITY: Belongs to the NGF-beta family.


Catalog Number: (10782-014)
Supplier: Biosensis
Description: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR) and upon binding to the receptor it induces the release of growth hormone from the pituitary. This ligand has an appetite-stimulating effect and is involved in growth regulation.


Catalog Number: (10782-008)
Supplier: Biosensis
Description: AGRP is the endogenous antagonist of alpha-melanocyte stimulating hormone and has been shown to cause potent stimulation of food intake, and this protein is found in over 90% of Neuropeptide Y containing cells in rats.


Catalog Number: (10782-000)
Supplier: Biosensis
Description: The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.


Catalog Number: (10781-962)
Supplier: Biosensis
Description: FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. SUBCELLULAR LOCATION: Endoplasmic reticulum; rough endoplasmic reticulum. Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. SIMILARITY: Belongs to the orexin family.


Catalog Number: (10781-982)
Supplier: Biosensis
Description: Uncoupling Protein 3 (UCP3) belongs to the mitochondrial carrier family. Located in the mitochondrion inner membrane, UCP3 creates proton leaks across the membrane thus uncoupling oxidative phosphorylation (Ref: SWISSPROT).


Catalog Number: (10782-390)
Supplier: Biosensis
Description: FUNCTION: Seems to promotes the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family.


Catalog Number: (10782-366)
Supplier: Biosensis
Description: FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.


Catalog Number: (10782-396)
Supplier: Biosensis
Description: FUNCTION: Target-derived survival factor for peripheral sensory sympathetic neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Highest levels in prostate, lower levels in thymus, placenta, and skeletal muscle. Expressed in embryonic and adult tissues. SIMILARITY: Belongs to the NGF-beta family.


Catalog Number: (10782-414)
Supplier: Biosensis
Description: FUNCTION: Required for autophagy. SUBUNIT: Conjugated to ATG5. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. SIMILARITY: Belongs to the ATG12 family.


Catalog Number: (10782-386)
Supplier: Biosensis
Description: FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Brain and peripheral tissues. SIMILARITY: Belongs to the NGF-beta family.


Catalog Number: (10782-942)
Supplier: Biosensis
Description: Peroxiredoxin-2 has a role in redox regulation of the cell.


Catalog Number: (10782-928)
Supplier: Biosensis
Description: Peripherin is a class-III neuronal intermediate filament protein found in certain classes of neuron, most of which are located in the peripheral nervous system.


Catalog Number: (10782-868)
Supplier: Biosensis
Description: Neurofilaments are composed of three intermediate filament proteins: light (~68 kDa), medium (~160 kDa) and heavy (~200 kDa), which are involved in the maintenance of the neuronal caliber. Neurofilament medium runs on SDS-PAGE gels in the range 145-170 kDa, with some variation in different species.


Catalog Number: (10782-876)
Supplier: Biosensis
Description: Vimentins are class-III intermediate filaments specific to mesenchymal tissue. Vimentin is an important cytoskeletal component responsible for maintaining cell integrity and has a probable role in the intracellular transport of proteins such as lipoproteins between the nucleus and plasma membrane. Immunohistochemical staining for Vimentin is characteristic of sarcomas. 


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