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Catalog Number: (BOSSBS-6433R-CY3)

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-HRP)

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-A750)

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-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-4735R-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 defence 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 defence 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-A647)

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

Sale

Catalog Number: (BOSSBS-4735R-CY3)

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

Sale

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-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

Sale

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

Sale

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

Sale

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

Sale

Catalog Number: (BOSSBS-1541R-CY7)

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-1541R-A680)

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

Sale