101316 Results for: "Cyclopropane-1,1-dicarboxylate+de+dim\u00E9thyle"

Supplier: HELLMA

Hellma® large cells for special applications in the Vis range, 10 to 50 mm path length, with or without lid.

Supplier: Bioss

IGSF11 is also known as BTIGSF (brain and testis-specific immunoglobulin superfamily protein) or VSIG3 (V-set and immunoglobulin domain-containing protein 3) and is a 431 amino acid protein that is expressed as three isoforms. IGSF11 is highly expressed in testis and ovary and is also expressed in brain, kidney and skeletal muscle, localized to the cellular membrane as a single-pass membrane protein. IGSF11 is an immunoglobulin with V-type and C2-type domains that function in molecular recognition. When IGSF11 is in the trans position, it plays an important role in cell-cell adhesion via both homophilic and heterophilic interactions with other molecules. These cell–cell interactions are also thought to be important for neuronal cell interactions, such as neuron–neuron or neuron–glia interactions, which are important for the development and function of the central nervous system. In addition, IGSF11 might also be involved interactions between Sertoli cells and spermatocytes, which are important associations during spermatogenesis. The IGSF11 gene is commonly upregulated in gastric cancer and IGSF11 is highly expressed in many types of human tumors, indicating that it may be useful as a target for immunotherapy.

Supplier: Bioss

Comprising more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdk1/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including CDC20, CDH1 and MAD2. Specifically, CDC20 and CDH1 directly bind to APC and activates APC’s cyclin-ubiquitination activity. In contrast, MAD2 inhibits APC by forming a ternary complex with CDC20 and APC; thus preventing APC activation. APC11 is a RING-H2 finger protein that allows for the synthesis of multiubiquitin chains in the presence of Ubiquitin carrier protein 4 (Ubc4) and ubiquitin conjugating enzyme (E2). In addition, a heterodimeric complex of either Ubc4 or UbcH10 with APC11 and APC2 catalyzes the ubiquitination of human securin and cyclin B1.

Supplier: Bioss

Comprising more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdk1/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including CDC20, CDH1 and MAD2. Specifically, CDC20 and CDH1 directly bind to APC and activates APC’s cyclin-ubiquitination activity. In contrast, MAD2 inhibits APC by forming a ternary complex with CDC20 and APC; thus preventing APC activation. APC11 is a RING-H2 finger protein that allows for the synthesis of multiubiquitin chains in the presence of Ubiquitin carrier protein 4 (Ubc4) and ubiquitin conjugating enzyme (E2). In addition, a heterodimeric complex of either Ubc4 or UbcH10 with APC11 and APC2 catalyzes the ubiquitination of human securin and cyclin B1.

Supplier: Bioss

Comprising more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdk1/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including CDC20, CDH1 and MAD2. Specifically, CDC20 and CDH1 directly bind to APC and activates APC’s cyclin-ubiquitination activity. In contrast, MAD2 inhibits APC by forming a ternary complex with CDC20 and APC; thus preventing APC activation. APC11 is a RING-H2 finger protein that allows for the synthesis of multiubiquitin chains in the presence of Ubiquitin carrier protein 4 (Ubc4) and ubiquitin conjugating enzyme (E2). In addition, a heterodimeric complex of either Ubc4 or UbcH10 with APC11 and APC2 catalyzes the ubiquitination of human securin and cyclin B1.

Supplier: ProSci Inc.

SHP2 Antibody: Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.

Supplier: ProSci Inc.

SPG11 Antibody: Hereditary spastic paraplegias (HSPs) are genetically and phenotypically heterogeneous disorders.  Spastic paraplegia with thinning of the corpus callosum (ARHSP-TCC) is a relatively frequent form of complicated hereditary spastic paraplegia (cHSP) in which mental retardation and muscle stiffness at onset are followed by slowly progressive paraparesis and cognitive deterioration. Mutations of the SPG11 gene encoding the spatacsin protein have been identified as a major cause of HSP-TCC. Spatacsin is a potential transmembrane protein that is phosphorylated upon DNA damage. It is expressed in all structures of the brain, with a high expression in the cerebellum. SPG11 mutations may occur more frequently in familial than sporadic forms of cHSP without TCC. Kjellin syndrome is found to be associated with mutations in not only the SPG15 gene but also SPG11 gene.  Recent studies show Parkinsonism may initiate SPG11-linked HSP TCC and that SPG11 may cause juvenile Parkinsonism.

Supplier: ProSci Inc.

CLDN11 belongs to the claudin family of tight junction associated proteins and is a major component of central nervous system myelin that is necessary for normal CNS function. There is growing evidence that the protein determines the permeability between layers of myelin sheaths via focal adhesion and, with its expression highly regulated during development, may play an important role in cellular proliferation and migration. In addition, the protein is a candidate autoantigen in the development of autoimmune demyelinating disease.The protein encoded by this gene belongs to the claudin family of tight junction associated proteins and is a major component of central nervous system myelin that is necessary for normal CNS function. There is growing evidence that the protein determines the permeability between layers of myelin sheaths via focal adhesion and, with its expression highly regulated during development, may play an important role in cellular proliferation and migration. In addition, the protein is a candidate autoantigen in the development of autoimmune demyelinating disease.

Supplier: ProSci Inc.

SHP2 Antibody: Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.

Supplier: ProSci Inc.

WBP11 is a nuclear protein, which colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks. WBP11has 95% amino acid sequence identity to the mouse Wbp11 protein. It contains two proline-rich regions that bind to the WW domain of Npw38, a nuclear protein, and thus this protein is also called Npw38-binding protein NpwBP. The Npw38-NpwBP complex may function as a component of an mRNA factory in the nucleus.This gene encodes a nuclear protein, which colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks. This protein has 95% amino acid sequence identity to the mouse Wbp11 protein. It contains two proline-rich regions that bind to the WW domain of Npw38, a nuclear protein, and thus this protein is also called Npw38-binding protein NpwBP. The Npw38-NpwBP complex may function as a component of an mRNA factory in the nucleus.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: CAMAG

CAMAG® TLC Visualizer 3 documentation system with 12 mm lens, without visionCATS software. Suited for object formats up to about 21×28 cm (20×20 cm TLC plates).

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: TRANE TECHNOLOGIES

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Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: HELLMA

Hellma® high precision quartz glass ultra-micro cell for absorption measurements in the UV/Vis range, 10 mm path length, with stopper.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.