You Searched For: Chloro(1,5-cyclooctadiene)rhodium+(I)+dimer


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Catalog Number: (BOSSBS-11126R-HRP)
Supplier: Bioss
Description: Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4. Functions as an entry receptor for herpes simplex virus and pseudorabies virus. Has some neurite outgrowth-promoting activity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6066R-A488)
Supplier: Bioss
Description: Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6066R-CY3)
Supplier: Bioss
Description: Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7559R-A750)
Supplier: Bioss
Description: Platelet-Derived Growth Factor (PDGF) is the major serum mitogen for cells of mesenchymal origin in humans. The biologically active protein is a dimer composed of two related polypeptides designated A and B. The PDGF protein has been implicated both directly as well as indirectly in several pathological states including neoplasia, arthritis, arteriosclerosis and bone marrow sclerosis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8286R-A647)
Supplier: Bioss
Description: The Dumpy-30 (DPY-30) protein was first described in C. elegans, in which it is involved in dosage compensation of sex chromosomes. Conserved from yeast to humans, the DPY-30 family is involved in gene expression and chromatin modification, specifically histone methylation. DPY-30 and closely related proteins contain a short motif that is related to the dimerization motif in the regulatory subunit of protein kinase A (PKA), which consists of two ?helices that form a four-helix bundle during dimerization. As a member of the DPY-30 family, DYDC1 (DPY30 domain-containing protein 1), also known as DPY30D1 and RSD9, is a 177 amino acid protein that binds to Endophilin III and plays a crucial role during acrosome biogenesis. DYDC1 is specifically expressed in brain and testis and accumulates in the acrosome area during spermatogenesis. Knockdown of DYDC1 mRNA results in disruption of acrosome formation and spermatid differentiation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8286R-FITC)
Supplier: Bioss
Description: The Dumpy-30 (DPY-30) protein was first described in C. elegans, in which it is involved in dosage compensation of sex chromosomes. Conserved from yeast to humans, the DPY-30 family is involved in gene expression and chromatin modification, specifically histone methylation. DPY-30 and closely related proteins contain a short motif that is related to the dimerization motif in the regulatory subunit of protein kinase A (PKA), which consists of two ?helices that form a four-helix bundle during dimerization. As a member of the DPY-30 family, DYDC1 (DPY30 domain-containing protein 1), also known as DPY30D1 and RSD9, is a 177 amino acid protein that binds to Endophilin III and plays a crucial role during acrosome biogenesis. DYDC1 is specifically expressed in brain and testis and accumulates in the acrosome area during spermatogenesis. Knockdown of DYDC1 mRNA results in disruption of acrosome formation and spermatid differentiation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11337R-CY7)
Supplier: Bioss
Description: C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorder characterized by lupus-like symptoms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11337R-A350)
Supplier: Bioss
Description: C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorder characterized by lupus-like symptoms.
UOM: 1 * 100 µl


Supplier: Biotium
Description: This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Biotium
Description: This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Biotium
Description: This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is located in the c-terminus of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Catalog Number: (BOSSBS-1025R-A555)
Supplier: Bioss
Description: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1025R-A488)
Supplier: Bioss
Description: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1025R-A647)
Supplier: Bioss
Description: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
UOM: 1 * 100 µl


Supplier: ENZO LIFE SCIENCES
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Supplier: ENZO LIFE SCIENCES
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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