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: 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: Description of target: Galectin-2 is a protein that in humans is encoded by the LGALS2 gene. It is mapped to 22q13.1. The protein encoded by this gene is a soluble beta-galactoside binding lectin. The encoded protein is found as a homodimer and can bind to lymphotoxin-alpha. It has been found that a single-nucleotide polymorphism in Galectin-2 is significantly associated with susceptibility to myocardial infarction.;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: <= 10 pg/mL

Description: Description of target: Angiopoietin-2 is a protein that in humans is encoded by the ANGPTL2 gene. Angiopoietins are members of the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietin-1, angiopoietin-2, and angiopoietin-4 participate in the formation of blood vessels. Human and mouse ANGPT2 are 85% identical in amino acid sequence and approximately 60% identical to their ANGPT1 homologs. Transgenic overexpression of ANGPT2 in mice disrupted blood vessel formation in the mouse embryo. By FISH and radiation hybrid analysis, the human ANGPT2 gene was mapped to 8p23, and in a region of syntenic homology on mouse chromosome 8, where the Angpt2 gene was mapped. ANGPT2 is a naturally occurring antagonist of angiopoietin-1 that competes for binding to the TIE2 receptor and blocks ANGPT1-induced TIE2 autophosphorylation during vasculogenesis .;Species reactivity: Mouse;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: <= 10 pg/mL

Description: Sealing film qPCR Optical (sticky adhesive film) Bio-Rad Type

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human PLIN - N-terminal region. This antibody is tested and proven to work in the following applications:

Description: Biotin is conjugated to NH2 group of S-adenosylmethionine.

Description: Biotin is conjugated to NH2 group of S-adenosylmethionine.

Description: Biotin is conjugated to NH2 group of S-adenosylhomocysteine.

Description: Biotin is conjugated to NH2 group of S-adenosylhomocysteine.