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cell+culture+flasks
Numéro de catalogue:
(BOSSBS-6661R-CY7)
Fournisseur:
Bioss
Description:
Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein aquaporins. Aquaporin 0 or MIP26 (major intrinsic protein 26kD), and Aquaporin 1 has been the foundation of the growing family of aquaporins. The lens specific Aquaporin 0 represents up to 80% of total lens membrane protein. Defects in Aquaporin 0 are a cause of autosomal recessive congenital cataract. The lens opacity mutation (LOP) is an AA substitution that inhibits targeting of MIP to the cell membrane. Human Aquaporin 0 is a 263 amino acid transmembrane protein belonging to the MIP family. Aquaporin families of proteins are predicted to contain six transmembrane domains. The N and C terminus are predicted to be cytoplasmic.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8697R-CY5.5)
Fournisseur:
Bioss
Description:
Connexin 29 belongs to the connexin family and is a member of the epsilon-type subfamily. Connexin 29 is a membrane bound, multi-pass protein also known as gap junction epsilon-1 protein. A connexon, consisting of connexin hexamers, is a membrane bound structure that is integral in the formation of a gap junction. One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low molecular weight diffuse from one cell to a neighboring cell. Connexin 29 expression is restricted to the central nervous system and is present in brain, spinal cord, and sciatic nerve samples. It has been suggested that connexin 29 in the mature CNS contributes minimally to gap junctional intercellular communication in oligodendrocyte cell bodies. Rather, connexin 29 is targeted to myelin where it, along with connexin 32, may contribute to connexin-mediated communication between adjacent layers of uncompacted myelin.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11080R-CY5)
Fournisseur:
Bioss
Description:
Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb reacts with a 58 kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Fournisseur:
Biotium
Description:
This MAb reacts with a 58 kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Numéro de catalogue:
(BOSSBS-13721R-CY3)
Fournisseur:
Bioss
Description:
The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including beta-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT4 (FAT tumor suppressor homolog 4), also known as FAT-J, CDHF14 or CDHR11, is a 4,981 amino acid single-pass type I membrane protein that belongs to the protocadherin subfamily of cadherins and localizes to the primary cilia of kidney. Widely expressed, FAT4 contains thirty-four cadherin domains, six EGF-like domains and two laminin G-like domains. FAT4 may function in the regulation of planar cell polarity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8080R-CY7)
Fournisseur:
Bioss
Description:
The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC58 (coiled-coil domain containing 58) is a 144 amino acid protein that is encoded by a gene that maps to human chromosome 3q21.1. Chromosome 3 is made up of about 214 million bases encoding over 1,100 genes. Notably, there is a chemokine receptor gene cluster and a variety of human cancer related loci on chromosome 3. Particular regions of the chromosome 3 short arm are deleted in many types of cancer cells. Key tumor suppressing genes on chromosome 3 encode apoptosis mediator RASSF1, cell migration regulator HYAL1 and angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth Disease are a few of the numerous genetic diseases associated with chromosome 3.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions. CD59 is widely distributed on cells in all tissues. The expression of CD59 on erythrocytes is important for their survival.
Numéro de catalogue:
(BNUM0629-50)
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions. CD59 is widely distributed on cells in all tissues. The expression of CD59 on erythrocytes is important for their survival.
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions.
Numéro de catalogue:
(BOSSBS-8364R)
Fournisseur:
Bioss
Description:
The regulated oscillation of protein expression is an essential mechanism of cell cycle control. The SCF class of E3 ubiquitin ligases is involved in this process by targeting cell cycle regulatory proteins for degradation by the proteasome, with the F-box subunit of the SCF specifically recruiting a given substrate to the SCF core. NIPA (nuclear interaction partner of ALK) is a human F-box-containing protein that defines an SCF-type E3 ligase (SCFNIPA) controlling mitotic entry. Assembly of this SCF complex is regulated by cell-cycle-dependent phosphorylation of NIPA, which restricts substrate ubiquitination activity to interphase. Nuclear cyclin B1 is a substrate of SCFNIPA. Inactivation of NIPA by RNAi results in nuclear accumulation of cyclin B1 in interphase, activation of cyclin B1-Cdk1 kinase activity, and premature mitotic entry. Thus, SCFNIPA-based ubiquitination may regulate S-phase completion and mitotic entry in the mammalian cell cycle.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions.
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions.
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions.
Fournisseur:
Biotium
Description:
Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein. CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb is useful for study on GPI-anchored proteins, PNH and CD59 functions.
Numéro de catalogue:
(BOSSBS-11752R-HRP)
Fournisseur:
Bioss
Description:
Transport of G protein-coupled receptors (GPCRs) to the cell surface membrane is critical for receptor-ligand recognition. Mammalian GPCR odorant receptors (ORs), when heterologously expressed in cells, are poorly expressed on the cell surface. REEP1 (receptor expression-enhancing protein 1), is a 201 amino acid multi-pass mitochondrion membrane protein that belongs to the DP1 family. REEP1 interacts with odorant receptor proteins and may enhance the cell surface expression of odorant receptors. Mutations in the REEP1 gene are the third most common cause of hereditary spastic paraplegia (HSP) after spastin and atlastin gene mutations. Mutations in the REEP1 gene also cause spastic paraplegia autosomal dominant type 31, a neurodegenerative disorder. The REEP1 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken, zebrafish, A.thaliana and rice, and maps to human chromosome 2p11.2.
UOM:
1 * 100 µl
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