You Searched For: Wound+Dressings

Catalog Number: (75976-656)

Supplier: Biotium

Description: This antibody recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Supplier: Peprotech

Description: SPARC/Osteonectin is a secreted, evolutionarily-conserved, collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains: an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant Human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation. The calculated molecular weight of Recombinant Human SPARC/Osteonectin is 32.7 kDa.

Catalog Number: (10423-264)

Supplier: Bioss

Description: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.

Catalog Number: (10072-614)

Supplier: Prosci

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β2 has been shown to exert suppressive effects on IL-2 dependent T-cell growth, and may also have an autocrine function in enhancing tumor growth by suppressing immuno-surveillance of tumor development. Recombinant human TGF-β2 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-β3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant Human TGF-β3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-β3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant Human TGF-β3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Catalog Number: (10464-400)

Supplier: Bioss

Description: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts, and recently it has been implicated in the formation of skin tumors. Recombinant Human TGF-β1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Catalog Number: (76303-590)

Supplier: Peprotech

Description: The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-beta3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant Human TGF-beta3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Catalog Number: (10464-388)

Supplier: Bioss

Description: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

Catalog Number: (10464-408)

Supplier: Bioss

Description: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

Catalog Number: (89158-460)

Supplier: Enzo Life Sciences

Description: Fibronectins are high molecular weight, disulphide-linked, dimeric cell adhesion glycoproteins found in basement membranes and in the interstitial connective tissue matrix. A single fibronectin gene is subject to alternative splicing in a cell-type-, development- and age-regulated manner which gives rise to multiple molecular forms. In addition to their prominent role in adhesion, fibronectins have been reported to mediate various aspects of cellular interaction, including migration during development and wound-healing, haemostasis, and the regulation of cell growth and differentiation. Cellular fibronectins (cFn) are found in low amounts in normal human plasma and tissues, but they are abundant in the plasma of carcinoma patients and in the stroma of various carcinomas. In contrast, a soluble form of fibronectin produced by hepatocytes is readily detectable in plasma and becomes deposited in pericellular matrices and within tissues. This form of fibronectin, referred to as ‘plasma fibronectin’ (pFn), differs from cFn by the absence of an amino acid sequence, known as extra domain A1.

Catalog Number: (10087-842)

Supplier: Proteintech

Description: GRN, also known as PGRN or PCDGF, is a cysteine-rich protein of 68.5 kDa that is typically secreted into a highly glycosylated 88 kDa form. PGRN is a unique growth factor that plays an important role in cutaneous wound healing. It has an anti-inflammatory effect and promotes cell proliferation. When PCDGF is degraded to several 6–25 kDa fragments, called granulins (GRNs) by neutrophil proteases, a pro-inflammatory reaction occurs. PGRN is widely expressed, particularly in epithelial cells, immune cells, neurons, and chondrocytes. High levels of PGRN expression have been reported in human cancers, and its expression is closely correlated with the development and metastasis of several cancers. The recent discovery that mutations in the gene encoding for pro-granulin (GRN) cause frontotemporal lobar degeneration (FTLD), and other neurodegenerative diseases leading to dementia, has brought renewed interest in progranulin and its functions in the central nervous system.

Supplier: Prosci

Description: The three mammalian isoforms of TGF-b, TGF-b1, b2, b3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-b isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-b1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts and recently it has been implicated in the formation of skin tumors. Recombinant human TGF-b1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Catalog Number: (MSPP-781861006)

Supplier: STEMCELL Technologies

Description: Fibroblast growth factor 7 (FGF-7) is a member of the FGF family, and acts exclusively through a subset of FGF receptor isoforms expressed predominantly by epithelial cells (Finch and Rubin). FGF-7 seems to act specifically on epithelial cells and stimulates proliferation, migration, and differentiation of these cells, and also participates in epithelial protection and repair both in vitro and in vivo (Finch and Rubin; Werner). In contrast, FGF-7 is produced solely by cells of mesenchymal origin, and functions as a paracrine mediator of mesenchymal-epithelial communication (Rubin <i>et al.</i>). FGF-7 has also been shown to supplement several wound-healing properties of bioengineered skin (Erdag <i>et al.</i>) and to induce autophagy in human keratinocytes (Belleudi <i>et al.</i>). Additionally, FGF-7 has a role in the differentiation of pluripotent stem cell to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami <i>et al.</i>; Niu <i>et al.</i>). This product is animal component-free.

New Product

Catalog Number: (10072-702)

Supplier: Prosci

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts and recently it has been implicated in the formation of skin tumors. Human TGF-β1 is a 25.0 kDa protein with each subunit containing 112 amino acid residues, linked by a single disulfide bond.