Aviva Bio Plin 2

Description: Description of target: ;Species reactivity: Pan-Species;Application: ;Assay info: Assay Methodology: Competitive Inhibition Immunoassay;Sensitivity: 1.41 ng/mL

Description: Description of target: Interleukin-2 (IL2), formerly referred to as T-cell growth factor, is a powerfully immunoregulatory lymphokine that is produced by lectin- or antigen-activated T cells. It is produced not only by mature T lymphocytes on stimulation but also constitutively by certain T-cell lymphoma cell lines. The lymphokine interleukin-2 (IL-2) is responsible for autocrine cell cycle progression and regulation of immune responses. IL-2 expression in mature thymocytes and T cells has been found to be tightly controlled by monoallelic expression.1 IL-2 can act as a growth hormone for both B and T lymphocytes.2 The human gene for interleukin 2 (IL2) is assigned to chromosome 4.3;Species reactivity: Rat;Application: ELISA;Assay info: ;Sensitivity: < 1 pg/ml

Description: Description of target: MIP is a member of the aquaporin family of membrane-bound water channels. MIP family proteins are thought to contain 6 TM domains. Sequence analysis suggests that the proteins may have arisen through tandem, intragenic duplication from an ancestral protein that contained 3 TM domains. Major intrinsic protein (MIP, also called MP26) is the predominant fiber cell membrane protein of the ocular lens. The major intrinsic protein (MIP) of the vertebrate eye lens is the first identified member of a sequence-related family of cell-membrane proteins that appears to have evolved by gene duplication. Several members of the MIP family transport water (aquaporins), glycerol and other small molecules in microbial, plant and animal cells. The standard used in this kit is recombinant mouse MIP-2(A28-N100), consisting of 73 amino acids with the molecular mass of 8KDa;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: < 5 pg/mL

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant human MMP-2, consisting of 631 amino acids with the molecular mass of 71KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/mL

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant mouse MMP-2, consisting of 662 amino acids with the molecular mass of 72KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/mL

Description: Description of target: TIMP2 gen is encoded by 5 exons spanning 83 kb of genomic DNA. TIMP2 is 83 kilobase pairs (kb) long with exon-intron splicing sites located in preserved positions among the three members of the TIMP family. The gene for tissue inhibitor of metalloproteinases-2 is localized on human chromosome arm 17q25. TIMP-2 abrogates angiogenic factor-induced endothelial cell proliferation in vitro and angiogenesis in vivo independent of MMP inhibition. The standard product used in this kit is recombinant human TIMP-2 with the molecular mass of 22Kda and 194 amino acid.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 2 pg/mL

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant rat MMP-2, consisting of 662 amino acids with the molecular mass of 72KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Rat;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/ml

Description: Description of target: HER2/neu (also known as ErbB-2) stands for "Human Epidermal growth factor Receptor 2" and is a protein giving higher aggressiveness in breast cancers. It is a member of the ErbB protein family, more commonly known as the epidermal growth factor receptor family. HER2/neu has also been designated as CD340 (cluster of differentiation 340) and p185. It is encoded by the ERBB2 gene.HER2 is a cell membrane surface-bound receptor tyrosine kinase and is normally involved in the signal transduction pathways leading to cell growth and differentiation. It is encoded within the genome by HER2/neu, a known proto-oncogene. HER2 is thought to be an orphan receptor, with none of the EGF family of ligands able to activate it. However, ErbB receptors dimerise on ligand binding, and HER2 is the preferential dimerisation partner of other members of the ErbB family.1 The HER2 gene is a proto-oncogene located at the long arm of human chromosome 17(17q21-q22)2.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/ml

Description: Biotin is conjugated to NH2 of SAM through 6-aminohexanoic acid.

Description: Biotin is conjugated to NH2 of SAM through 6-aminohexanoic acid.

Description: Biotin is conjugated to NH2 of SAH through 6-aminohexanoic acid.

Description: Biotin is conjugated to NH2 of SAH through 6-aminohexanoic acid.

Description: Biotin is conjugated to NH2 of SAH through a 10-carbon and 2-nitrogen linker.

Description: Biotin is conjugated to NH2 of SAH through a 10-carbon and 2-nitrogen linker.

Description: Biotin is conjugated to NH2 of SAH through a 10-carbon and 2-nitrogen linker.

Description: GSK-3 inhibitor IX (BIO) is a potent, selective, cell-permeable, ATP-competitive and reversible inhibitor of GSK-3? (glycogen synthase kinase-3?) and GSK-3? (lycogen synthase kinase-3?) (IC50 = 5nM for GSK-3?).