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Fournisseur: MP Biomedicals
Description: Bromelain is a glycoprotein which is a highly active thiol proteinase (non-specific cysteine protease), which splits glycine esters but not lysine esters; it is also a protein-digesting and milk-clotting enzyme. Substrates susceptible to bromelain include all of the common protein materials such as gelatin, casein, gluten, collagen, elastin, globulins an muscle fiber protein. It is a cysteine endopeptidase with broad specificity for cleavage of proteins. It may be from a stem or piece of fruit.

Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Numéro de catalogue: (BNUM0918-50)
Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.
UOM: 1 * 50 µl


Numéro de catalogue: (ROCKMB-104-0500)
Fournisseur: Rockland Immunochemicals
Description: Lambda phage consists of a virus particle including a head (also known as a capsid), a tail and tail fibres. The head contains the phage's double-stranded circular DNA genome. The phage particle recognises and binds to its host <i>E.coli</i> causing DNA in the head of the phage to be ejected through the tail into the cytoplasm of the bacterial cell. Lambda phage DNA is commonly used as a DNA molecular weight marker. Digestion of the lambda phage genome with HindIII produces a set of 8 fragments consisting of 125, 560, 2000, 2300, 4300, 9400, and 23000 base pairs.
UOM: 1 * 500 µG


Numéro de catalogue: (BOSSBS-12933R-A750)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyse other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesised in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-12933R-HRP)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-12933R-FITC)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Numéro de catalogue: (PRSI92-321)
Fournisseur: ProSci Inc.
Description: Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle materials when they are no longer needed. Cathepsin A interacts with the enzymes beta -galactosidase and neuraminidase 1, which play a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) or fats (glycolipids). Cathepsin A forms a complex with these two enzymes and directs their transport within the cell to the lysosomes. Within lysosomes, cathepsin A activates the enzymes and prevents their breakdown.
UOM: 1 * 50 µG


Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Fournisseur: Biotium
Description: Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes (Leucocyte Typing Workshop V). Its epitope is resistant to digestion by trypsin and chymotrypsin. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Numéro de catalogue: (BOSSBS-12933R-A488)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-12933R-A647)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-12933R-A555)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


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