24517 Results for: "734-0023%20"

Supplier: Binder

The MK series chambers are suitable for all heat and cold tests from –40 to 180 °C. This is an alternative to complex individual solutions for cyclical temperature tests.

Supplier: Binder

Standard climate chambers that work with APT.line™ preheating chamber technology.

Supplier: VWR Collection

These protecting covers for clamp jaws are made from red vinyl.

Supplier: Thermo Fisher Scientific

PS (except 734-2113*, made of Permanox™), sterile, with lid. A large range of dishes, which have been tissue culture-treated.

Supplier: Brady

This box accommodates 8 to 10 locks (depending on lock size).

Supplier: ENTEGRIS

These tube fittings are made from PFA.

Supplier: Binder

The MFK series of dynamic climate chambers has been specially developed as precision heating and cooling chambers for complex standards-based climatic testing. The units are ideal for rapid temperature changes with humidity control with a low temperature range down to –70 °C and have a higher capacity which exceeds the capability of normal testing chambers. The stainless steel inner chamber has door heating, a heated viewing window with LED interior lighting and programmable condensation protection for the test materials.

Supplier: Hach

Electrolyte solution 0,1 M, 125 ml, for sensION+ ISE for sodium ion in range 0,023 - 23000 mg/lL

Supplier: Merck

RiOs™ systems are used to produce large volumes of Type 3 water from potable tap water. The RiOs™ system incorporates both the complete water purification sequence for the production of laboratory-grade water, as well as the entire control and monitoring functions for the total water purification system. Flow rate and water quality can be upgraded in RiOs™ systems.

Supplier: Bioss

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.

Supplier: Binder

Avantgarde. Line incubators ensure stable and reliable incubation of microbiological cultures and guarantee reproducible results for routine tests in the laboratory – even high batch throughputs and with long-term operation. Avantgarde. Line BD models have natural convection ensuring rapid temperature equalisation after the door is opened. The BF models have forced convection via a fan. The APT.line™ pre-heating chamber technology gives homogeneous temperature distribution, excellent temperature uniformity and low fluctuation. Units up to 115 litres can be stacked on top of each other to save space. The units have 60 mm insulation which lowers energy consumption and increases performance. All models have a stainless steel chamber with an ergonomic door opening system.

Supplier: Agilent

These nebulisers for PerkinElmer AA systems provide the best precision, efficient drainage, minimal burner blockage, and reduced interferences.

Supplier: HIRSCHMANN

AR-Glas®

Supplier: Binder

The MKF series of dynamic climate chambers has been specially developed as precision heating and cooling chambers for industrial material testing and environment simulation applications. The units are ideal for rapid temperature changes with humidity control and have a higher capacity which exceeds the capability of normal testing chambers. The stainless steel inner chamber has door heating, a heated viewing window with LED interior lighting and programmable condensation protection for the test materials.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: BEHR

For the determination of readily liberated cyanides, the DET basic unit (DBAS, 705-0023) and the supplementary set for total cyanides (DGC, 705-0024) are also required together with the DLFC set.
The DLFC set includes the following equipment:

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: KARTELL

Rinsing sets for cleaning pipettes up to 600 mm length and Mohr burettes gently and efficiently. The entire washing system consists of a washer, a pipette jar and a pipette basket.

Supplier: Portwest

Contemporary work trouser made from highly durable ripstop fabric that stretches as you move. Subtle articulation on the knees allow for increased freedom of movement and a high rise back waistband ensures protection in all working positions. Packed with functionality including pre-bent knees, a crotch gusset, two tier knee pad pockets and an adjustable leg length for added convenience.

Supplier: Avantor

Polysorbate 20, Multi-Compendial, J.T.Baker®