Esta buscando: Eshmuno\u00AE+CPX

Proveedor: MERCK PRODUCTION CHEMICALS

Descripción: Eshmuno® CPX media is a strong cation exchanger built on the proven Eshmuno® resin technology.

FDS

Numero del catalogo: (BOSSBS-8331R-CY7)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-A555)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-A647)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-CY5.5)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-HRP)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-A680)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-A350)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-CY5)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-HRP)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-CY5)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8331R-CY3)

Proveedor: Bioss

Descripción: CPXCR1 is widely expressed in fetal tissues, including the tongue, mandible and palate with an unknown function. Cleft palate most commonly occurs as a sporadic multifactorial disorder with a clear but difficult to define genetic component. As a semi-dominant disorder, X-linked cleft palate (CPX) provides a useful model to investigate a congenital defect that is little influenced by non-genetic factors.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-CY5.5)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-A555)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción