You Searched For: Wound+Dressings

Catalog Number: (BOSSBS-1541R-A488)

Supplier: Bioss

Description: Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodelling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6505R-A680)

Supplier: Bioss

Description: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerisation which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6433R-FITC)

Supplier: Bioss

Description: Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6433R-CY7)

Supplier: Bioss

Description: Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6433R-A680)

Supplier: Bioss

Description: Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in -pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4735R-A488)

Supplier: Bioss

Description: Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1862R-A555)

Supplier: Bioss

Description: The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1862R-CY5)

Supplier: Bioss

Description: The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6433R-A555)

Supplier: Bioss

Description: Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

UOM: 1 * 100 µl

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Catalog Number: (PRSI92-639)

Supplier: ProSci Inc.

Description: NOV, also called CCN3, is a secreted protein of CCN family members. CCN family members are highly conserved cysteine rich proteins sharing a common modular structure having 4 conserved domains, insulin-like growth factor-binding protein (IGFBP) domain, von Willebrand type C (VWC) domain, thrombospondin-1 (TSP-1) domain, and C-terminal (CT) domain (absent in CCN5). By specific interactions with these domains, CCN proteins modulate multiple signalling pathways including BMPs, Wnt, TGFs, Notch and integrins to regulate cell proliferation, differentiation, adhesion, migration, angiogenesis, and survival. CCN3 is firstly characterised as a promoter of progenitor activity of human hematopoietic stem cells, as knockdown of CCN3 can abrogate the function of primitive progenitors. Recent studies showed that CCN3 is also actively involved in the process of wound healing. CCN3 is highly expressed in granulation tissues of cutaneous wounds and capable of inducing synthetic responses of fibroblasts.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-0668R-A680)

Supplier: Bioss

Description: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodelling. Promotes also differentiation and proliferation of hematopoietic cells. Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.

UOM: 1 * 100 µl

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Catalog Number: (BINH1005683)

Supplier: 3B Scientific

Description: Made with a soft vinyl skin over a core of stitchable foam to provide a lifelike suturing experience for students or a realistic suturing demonstration by an instructor. Realistic skin texture with wrinkles and pores. Soft and pliable for easy sewing, the skin is tough enough that sutures will not pull out when tightened. Each unit provides three 'wounds'. These 'wounds' can be sutured repeatedly until the skin around them is finally worn out; then, new 'wounds' can be cut. Although disposable, the trainers provides hundreds of suturing experiences before wearing out. Conservatively, over one hundred cuts can be made on the trainer and each of these cuts can be sutured several times.

UOM: 1 * 1 items

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Catalog Number: (PRSI91-020)

Supplier: ProSci Inc.

Description: Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell growth, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), which is a competitor for EGF receptor sites. EGF is a small 53 amino acid residue long protein that contains three disulfide bridges

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-1703R-A350)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1703R-CY7)

Supplier: Bioss

Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0801R-CY7)

Supplier: Bioss

Description: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity).

UOM: 1 * 100 µl

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