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Proteine+und+Peptide


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Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2374R-CY7
Lokale Artikelnummer:: BOSSBS-2374R-CY7
Beschreibung:   TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2374R-A750
Lokale Artikelnummer:: BOSSBS-2374R-A750
Beschreibung:   TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-1559R-A555
Lokale Artikelnummer:: BOSSBS-1559R-A555
Beschreibung:   This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2374R-A488
Lokale Artikelnummer:: BOSSBS-2374R-A488
Beschreibung:   TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5912R-A350
Lokale Artikelnummer:: BOSSBS-5912R-A350
Beschreibung:   PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5912R-HRP
Lokale Artikelnummer:: BOSSBS-5912R-HRP
Beschreibung:   PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-7800R-A350
Lokale Artikelnummer:: BOSSBS-7800R-A350
Beschreibung:   The GLP2 receptor (GLP2R) is a G protein-coupled receptor superfamily member closely related to the glucagon receptor ans GLP1 receptor. Glucagon-like peptide-2 (GLP2) is a 33-amino acid proglucagon-derived peptide produced by intestinal enteroendocrine cells. Like glucagon-like peptide-1 (GLP1) and glucagon itself, it is derived from the proglucagon peptide encoded by the GCG gene. GLP2 stimulates intestinal growth and upregulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP2 prevents intestinal hypoplasia resulting from total parenteral nutrition. GLP2R, a G protein-coupled receptor superfamily member is expressed in the gut and closely related to the glucagon receptor (GCGR) and the receptor for GLP1 (GLP1R). [provided by RefSeq, Jul 2008].
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-7800R-CY3
Lokale Artikelnummer:: BOSSBS-7800R-CY3
Beschreibung:   The GLP2 receptor (GLP2R) is a G protein-coupled receptor superfamily member closely related to the glucagon receptor ans GLP1 receptor. Glucagon-like peptide-2 (GLP2) is a 33-amino acid proglucagon-derived peptide produced by intestinal enteroendocrine cells. Like glucagon-like peptide-1 (GLP1) and glucagon itself, it is derived from the proglucagon peptide encoded by the GCG gene. GLP2 stimulates intestinal growth and upregulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP2 prevents intestinal hypoplasia resulting from total parenteral nutrition. GLP2R, a G protein-coupled receptor superfamily member is expressed in the gut and closely related to the glucagon receptor (GCGR) and the receptor for GLP1 (GLP1R). [provided by RefSeq, Jul 2008].
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-7800R-A680
Lokale Artikelnummer:: BOSSBS-7800R-A680
Beschreibung:   The GLP2 receptor (GLP2R) is a G protein-coupled receptor superfamily member closely related to the glucagon receptor ans GLP1 receptor. Glucagon-like peptide-2 (GLP2) is a 33-amino acid proglucagon-derived peptide produced by intestinal enteroendocrine cells. Like glucagon-like peptide-1 (GLP1) and glucagon itself, it is derived from the proglucagon peptide encoded by the GCG gene. GLP2 stimulates intestinal growth and upregulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP2 prevents intestinal hypoplasia resulting from total parenteral nutrition. GLP2R, a G protein-coupled receptor superfamily member is expressed in the gut and closely related to the glucagon receptor (GCGR) and the receptor for GLP1 (GLP1R).
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2789R-A350
Lokale Artikelnummer:: BOSSBS-2789R-A350
Beschreibung:   Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2789R-FITC
Lokale Artikelnummer:: BOSSBS-2789R-FITC
Beschreibung:   Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-2789R-A647
Lokale Artikelnummer:: BOSSBS-2789R-A647
Beschreibung:   Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-4735R-CY7)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-4735R-CY7
Lokale Artikelnummer:: BOSSBS-4735R-CY7
Beschreibung:   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.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-6433R-A647
Lokale Artikelnummer:: BOSSBS-6433R-A647
Beschreibung:   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.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-4735R-A750
Lokale Artikelnummer:: BOSSBS-4735R-A750
Beschreibung:   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.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-1724R-A680
Lokale Artikelnummer:: BOSSBS-1724R-A680
Beschreibung:   Motilin is a 22 amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract. The protein encoded by this gene is a motilin receptor which is a member of the G-protein coupled receptor 1 family. This member is a multi-pass transmembrane protein, and is an important therapeutic target for the treatment of hypomotility disorders.
VE:  1 * 100 µl
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