16635 Results for: "1,1'-(2,6-pyridinediol)bis(3-methylimidazolium)dibromide"

Supplier: Tonbo Biosciences

The O323 antibody reacts with human CD27 (TNFRSF7), a cell surface homodimer of 55 kDa subunits, which provides co-stimulatory signaling in support of the T cell (TCR) and B cell (BCR) receptors. By comparison with CD28, whose TCR co-stimulatory signal can trigger cell proliferation, CD27 signaling appears to promote cell survival and differentiation to effector / memory stages. Also in contrast with CD28, the CD27 receptor may be shed following interaction with its ligand CD70, which is typically expressed on activated dendritic cells, T cells and B cells. With respect to B cells, CD27 is considered to be a phenotypic marker for memory B cells. CD27 has been included within a group of phenotypic markers for identifying human B regulatory cells (Bregs), a cell type proposed to regulate CD4+ T cell proliferation and Foxp3 / CTLA-4 expression in Treg cells.

Supplier: Simport Scientific

The Simport CryoSette™ is designed for frozen tissue collection, transport and storage. It can also be used for storing a multitude of other specimens in all laboratories. The robust design of the cryosette ensures that tissue morphology will be well preserved.

Supplier: Bioss

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

Supplier: Prosci

Interleukin-33 (IL-33) was initially discovered as a nuclear factor NF-HEV abundantly expressed in high endothelial venules. It is a 30-32 kD pro-inflammatory protein with intracellular and extracellular activities and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 is highly and selectively expressed by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyers's patches, and lymph nodes. It contains a bipartite nuclear localization signal at the C-terminus, and is targeted to the nucleus when ectopically expressed in human umbilical vein endothelial cells (HUVECs) and HeLa cells. The C-terminal fragment, corresponding to mature IL-33, binds and triggers signaling. IL-33 mediates its biological effects via Toll-interleukin 1 (IL-1) receptor (TIR) domain-containing receptor ST2, activates NF-kappaB and MAP kinases, and drives production of T(H)2-associated cytokines from in vitro polarized T(H)2 cells. In vivo, IL-33 induces the expression of IL-4, IL-5, and IL-13 and leads to severe pathological changes in mucosal organs. Human IL-33 is 270 amino acids in length.

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: MOLECULAR DEVICES LLC. CA

Unparalleled performance on a personalized platform. The SpectraMax® iD3 Multi-Mode Microplate Reader is the cornerstone of a complete laboratory solution designed to expand the boundaries of research capabilities. With optimized reagents and the industry-leading data acquisition and analysis tool, SoftMax Pro® 7 Software, the SpectraMax® iD3 allows users to customize workflow to perfectly match their needs.

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

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

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: Corning

These kits are ideal for standard laboratory experiments.

Supplier: Tonbo Biosciences

The O323 antibody reacts with human CD27 (TNFRSF7), a cell surface homodimer of 55 kDa subunits, which provides co-stimulatory signaling in support of the T cell (TCR) and B cell (BCR) receptors. By comparison with CD28, whose TCR co-stimulatory signal can trigger cell proliferation, CD27 signaling appears to promote cell survival and differentiation to effector / memory stages. Also in contrast with CD28, the CD27 receptor may be shed following interaction with its ligand CD70, which is typically expressed on activated dendritic cells, T cells and B cells. With respect to B cells, CD27 is considered to be a phenotypic marker for memory B cells. CD27 has been included within a group of phenotypic markers for identifying human B regulatory cells (Bregs), a cell type proposed to regulate CD4+ T cell proliferation and Foxp3 / CTLA-4 expression in Treg cells.

Supplier: Greiner Bio-One

Blood collection sets are designed to increase the safety of routine venipuncture procedures.

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

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

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: VWR International

Advanced magnetic hotplate stirrers are designed to deliver accurate and repeatable results in all research, academic, and industrial applications. With temperature ranges up to 500 °C and stirring speeds reaching 1600 rpm, the VWR® hotplate stirrers provides proper mixing and superior temperature control. Available in three sizes and a choice of two top plate materials.

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

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

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

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: Cytiva

rProtein A Sepharose™ 4 Fast Flow is a well established antibody affinity medium is designed for the purification of monoclonal and polyclonal antibodies based on Sepharose™ Fast Flow platform. The recombinant protein A is produced in E.coli and engineered for an oriented coupling to giving a matrix with enhanced binding capacity. The epoxy-based coupling ensures low ligand leakage. The specificity of the recombinant protein A for the Fc region of IgG is similar to native protein A and provides excellent purification in one step. The high capacity, low ligand leakage and a well established base matrix makes rProtein A Sepharose™ Fast Flow ideal for purification of monoclonal antibodies at both laboratory and process scale.

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: Genetex

The serum amyloid A (SAA) family comprises a number of differentially expressed lipoproteins, acute-phase SAA1 and SAA2, the former being a major component in plasma, and constitutive SAA's (C-SAAs). Although the liver is the primary site of synthesis of both SAA types, extrhepatic production has been reported. The in-vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed it's importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations. SAA rises earlier and more sharply than CRP.SAA enhances the binding of HDL's to macrophages and thus helps the delivery of lipid to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease process. In addition, recent experiments suggest that SAA may play a "houekeeping" role in normal human tissues.Elevated levels of SAA over time predispose secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissues and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid artheritis.

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: Zymo Research

The Zymo-Spin P-96 plate can be used with centrifuges and vacuum manifolds for large-scale (96-well) purification of plasmid DNA.