Esta buscando: Aflatoxin+B2

Numero del catalogo: (PRSI79-925)

Proveedor: ProSci Inc.

Descripción: This gene encodes a member of the tob/btg1 family of anti-proliferative proteins that have the potential to regulate cell growth. When exogenously expressed, this protein supresses cell growth in tissue culture. The protein undergoes phophorylation by a serine/threonine kinase, 90 kDa ribosomal S6 kinase. Interactions of this protein with the v-erb-b2 erythroblastic leukemia viral oncogene homolog 2 gene product p185 interferes with growth suppression. This protein inhibits T cell proliferation and transcription of cytokines and cyclins. The protein interacts with both mothers against decapentaplegic Drosophila homolog 2 and 4 to enhance their DNA binding activity. This interaction inhibits interleukin 2 transcription in T cells.

UOM: 1 * 100 µG

Promoción

Numero del catalogo: (BOSSBS-7547R-CY7)

Proveedor: Bioss

Descripción: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-7547R-CY5.5)

Proveedor: Bioss

Descripción: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11281R-A750)

Proveedor: Bioss

Descripción: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date. While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development. The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-7547R-A750)

Proveedor: Bioss

Descripción: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11281R-A680)

Proveedor: Bioss

Descripción: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date. While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development. The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A750)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukaemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A680)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukaemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-13275R-HRP)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of clathrin binding adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP180 (also designated AP-3 or F1-20) is a synapse-specific clathrin assembly protein. The protein CALM (clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A350)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A555)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A647)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-A488)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11333R-FITC)

Proveedor: Bioss

Descripción: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BSENR-1697-100)

Proveedor: Biosensis

Descripción: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11281R-CY3)

Proveedor: Bioss

Descripción: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

UOM: 1 * 100 µl

Promoción