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acids+and+salts+high+purity
Numéro de catalogue:
(BOSSBS-4965R-A488)
Fournisseur:
Bioss
Description:
The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4965R-A350)
Fournisseur:
Bioss
Description:
The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4965R-A647)
Fournisseur:
Bioss
Description:
The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8579R-A555)
Fournisseur:
Bioss
Description:
The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4894R-A750)
Fournisseur:
Bioss
Description:
Catalyses the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4894R-HRP)
Fournisseur:
Bioss
Description:
Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.
UOM:
1 * 100 µl
Numéro de catalogue:
(BSENC-1807-50)
Fournisseur:
Biosensis
Description:
Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface (PubMed:27362226). Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization (PubMed:24867636). It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed (Probable). Ref: uniprot.org
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-11954R)
Fournisseur:
Bioss
Description:
Myo-inositol is involved in many important aspects of cellular regulation including membrane structure, signal transduction and osmoregulation. It is taken up into cells by the sodium/myo-inositol cotransporter (SMIT). SMIT activity maintains intracellular concentrations of myo-inositol; it is upregulated in response to hypertonic stress. The human SMIT protein is encoded by the SLC5A3 gene, which maps to chromosome 21q22.12. It is expressed in many human tissues, such as brain, kidney and placenta. Specifically, SMIT is abundantly expressed throughout the whole brain and spinal cord in fetal rat, but is downregulated in adult rat brain with the exception of the choroid plexus, where SMIT expression remains high. In kidney, SMIT localizes to the baso-lateral membranes of the thick ascending limb of Henle (TAL) and the inner medullary collecting duct (IMCD). Impaired SMIT activity is implicated in the pathogenesis of diabetes and Down syndrome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7649R)
Fournisseur:
Bioss
Description:
Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. DFF45/ICARD has been identified as inhibitor of caspase activated DNase DFF40/CAD. DFF45 related proteins CIDE A and CIDE B (for cell death inducing DFF like effector A and B) were recently identified. CIDE contains a new type of domain termed CIDE N, which has high homology with the regulatory domains of DFF45/ICAD and DFF40/CAD. Expression of CIDE A induces DNA fragmentation and activates apoptosis, which is inhibited by DFF45. CIDE A is a DFF45 inhibitable effector that promotes cell death and DNA fragmentation. CIDE A is expressed in many tissues.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10065R-A555)
Fournisseur:
Bioss
Description:
Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin signaling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins, as the cells are repelled, rather than attracted, by the netrin gradient. Netrin-4 is related to the Laminin ∫ chains, and is therefore also designated ∫-netrin. It is present in the basement membranes of the vasculature, lateral olfactory tract, kidney and ovary. In humans, the gene encoding for the netrin-4 protein is localized to chromosome 12q22-q23. High levels of netrin-4 mRNA have also been detected in many cells and tissues, including cerebral cortex, hippocampus, amygdaloid nuclei and Purkinje cells. Netrin-4 is important in neural, kidney and vascular development.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Cytokeratin 8 (CK8) belongs to the type II (or B or basic) subfamily of high molecular weight cytokeratins and exists in combination with cytokeratin 18 (CK18). CK8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin 8 and 18. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular (ring-like, perinuclear) from ductal (peripheral-predominant) carcinoma of the breast.
Fournisseur:
Biotium
Description:
Cytokeratin 8 (CK8) belongs to the type II (or B or basic) subfamily of high molecular weight cytokeratins and exists in combination with cytokeratin 18 (CK18). CK8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin 8 and 18. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular (ring-like, perinuclear) from ductal (peripheral-predominant) carcinoma of the breast.
Fournisseur:
Biotium
Description:
Cytokeratin 8 (CK8) belongs to the type II (or B or basic) subfamily of high molecular weight cytokeratins and exists in combination with cytokeratin 18 (CK18). CK8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin 8 and 18. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular ring-like, perinuclear from ductal peripheral-predominant carcinoma of the breast.
Numéro de catalogue:
(BSENM-1805-100)
Fournisseur:
Biosensis
Description:
Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface (PubMed:27362226). Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization (PubMed:24867636). It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed (Probable). Ref: uniprot.org
UOM:
1 * 1 EA
Numéro de catalogue:
(BOSSBS-1476R-CY5)
Fournisseur:
Bioss
Description:
This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11954R-A555)
Fournisseur:
Bioss
Description:
Myo-inositol is involved in many important aspects of cellular regulation including membrane structure, signal transduction and osmoregulation. It is taken up into cells by the sodium/myo-inositol cotransporter (SMIT). SMIT activity maintains intracellular concentrations of myo-inositol; it is upregulated in response to hypertonic stress. The human SMIT protein is encoded by the SLC5A3 gene, which maps to chromosome 21q22.12. It is expressed in many human tissues, such as brain, kidney and placenta. Specifically, SMIT is abundantly expressed throughout the whole brain and spinal cord in fetal rat, but is downregulated in adult rat brain with the exception of the choroid plexus, where SMIT expression remains high. In kidney, SMIT localizes to the baso-lateral membranes of the thick ascending limb of Henle (TAL) and the inner medullary collecting duct (IMCD). Impaired SMIT activity is implicated in the pathogenesis of diabetes and Down syndrome.
UOM:
1 * 100 µl
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