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Hai cercato: Neu5Ac-alpha(2-3)Gal-beta-MP+Glycoside


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Codice catalogo: (BOSSBS-5855R-CY5.5)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R-CY5.5
Codice articolo locale: BOSSBS-5855R-CY5.5
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-5855R-FITC)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R-FITC
Codice articolo locale: BOSSBS-5855R-FITC
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


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Codice catalogo: (BOSSBS-5855R-HRP)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R-HRP
Codice articolo locale: BOSSBS-5855R-HRP
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-5855R-A750)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R-A750
Codice articolo locale: BOSSBS-5855R-A750
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilisation. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


Fornitore: MP Biomedicals
Descrizione: Streptomycin sulphate is an aminoglucoside antibiotic in which streptidine is linked glycosidically to the disaccharide streptobiosamine. It is used to inhibit bacterial protein synthesis at the level of initiation inhibition. It inhibits gram-negative and gram-positive bacteria.

Codice catalogo: (BOSSBS-5855R-CY5)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R-CY5
Codice articolo locale: BOSSBS-5855R-CY5
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-5855R)
Fornitore: Bioss
Codice articolo fornitore: BS-5855R
Codice articolo locale: BOSSBS-5855R
Descrizione: ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
UOM: 1 * 100 µl


Fornitore: Apollo Scientific
Descrizione: 6-Chloro-3-indolyl-α-D-galactopyranoside

Fornitore: Apollo Scientific
Descrizione: Salmon-XGlcA is an alternative substrate for b-Glucuronidase (GUS) encoded by the gusA gene. In conjunction with X-Gal, useful for simultaneous detection of Gus and Lac activities on the same plate.

Fornitore: Apollo Scientific
Descrizione: 5-Bromo-6-chloro-3-indolyl α-D-galactopyranoside

Codice catalogo: (PRSI91-719)
Fornitore: ProSci Inc.
Codice articolo fornitore: 91-719
Codice articolo locale: PRSI91-719
Descrizione: Lysozyme G-Like Protein 2 (LYG2) is a secreted protein that belongs to the glycosyl hydrolase 23 family. LYG2 contains one SLT domain, one protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta -1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc). LYG2 has hydrolase activity which acting on glycosyl bonds, and possess lysozyme activity.
UOM: 1 * 50 µG


Codice catalogo: (PRSI6947)
Fornitore: ProSci Inc.
Codice articolo fornitore: 6947
Codice articolo locale: PRSI6947
Descrizione: LYZL1 Antibody: The lysozyme family of proteins has an important role in host defense and is associated with the monocyte-macrophage system and enhances the activity of immunoagents. The mammalian lysozyme gene family is much larger than previously appreciated and consists of at least eight distinct genes scattered around the genome. C-type lysozymes are specifically involved catalyzing the hydrolysis of beta -1,4 glycosidic bonds of the peptidoglycan of bacterial cell walls. As a homolog of human C-type lysozyme, LYZL1 is an intra-acrosomal, nonbacteriolytic, c lysozyme-like protein recently isolated from human spermatozoa.
UOM: 1 * 100 µG


Codice catalogo: (BOSSBS-2807R-HRP)
Fornitore: Bioss
Codice articolo fornitore: BS-2807R-HRP
Codice articolo locale: BOSSBS-2807R-HRP
Descrizione: Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N-acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-8032R-A555)
Fornitore: Bioss
Codice articolo fornitore: BS-8032R-A555
Codice articolo locale: BOSSBS-8032R-A555
Descrizione: COLEC11 is a 271 amino acid C-type lectin protein that contains a collagen-like domain and a carbohydrate recognition domain, and plays an important role in host-defense. COLEC11 binds to various sugars and LPS (lipopolysaccharides), which include fucose but does not bind to glucose, hnRNP, Beta-1,3-Gal-T3 or mannose. COLEC11 is ubiquitously expressed in most tissues with high expression in kidney, liver, fetal liver, small intestine, thymus, spinal cord, placenta, adrenal gland, pancreas and several cell lines. COLEC11 is a secreted protein and all alternatively spliced isoforms of COLEC11 have oligomeric structures created through disulfide bonding.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-8032R-CY7)
Fornitore: Bioss
Codice articolo fornitore: BS-8032R-CY7
Codice articolo locale: BOSSBS-8032R-CY7
Descrizione: COLEC11 is a 271 amino acid C-type lectin protein that contains a collagen-like domain and a carbohydrate recognition domain, and plays an important role in host-defense. COLEC11 binds to various sugars and LPS (lipopolysaccharides), which include fucose but does not bind to glucose, hnRNP, Beta-1,3-Gal-T3 or mannose. COLEC11 is ubiquitously expressed in most tissues with high expression in kidney, liver, fetal liver, small intestine, thymus, spinal cord, placenta, adrenal gland, pancreas and several cell lines. COLEC11 is a secreted protein and all alternatively spliced isoforms of COLEC11 have oligomeric structures created through disulfide bonding.
UOM: 1 * 100 µl


Codice catalogo: (BOSSBS-8032R-CY5)
Fornitore: Bioss
Codice articolo fornitore: BS-8032R-CY5
Codice articolo locale: BOSSBS-8032R-CY5
Descrizione: COLEC11 is a 271 amino acid C-type lectin protein that contains a collagen-like domain and a carbohydrate recognition domain, and plays an important role in host-defense. COLEC11 binds to various sugars and LPS (lipopolysaccharides), which include fucose but does not bind to glucose, hnRNP, Beta-1,3-Gal-T3 or mannose. COLEC11 is ubiquitously expressed in most tissues with high expression in kidney, liver, fetal liver, small intestine, thymus, spinal cord, placenta, adrenal gland, pancreas and several cell lines. COLEC11 is a secreted protein and all alternatively spliced isoforms of COLEC11 have oligomeric structures created through disulfide bonding.
UOM: 1 * 100 µl


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