Description: Sum Formula: C6H8N2O2; CAS# [1074-59-5]

Description: HDC (Histidine decarboxylase) is the enzyme that catalyzes the reaction that produces histamine from histidine with the help of vitamin B6. The HDC gene is mapped on 15q21.2. The deduced 662-amino acid protein has a molecular mass of 74,148 Da. The gene contains 12 exons spanning approximately 24 kb. The biogenic amine histamine is an important modulator of numerous physiologic processes, including neurotransmission, gastric acid secretion, and smooth muscle tone. The biosynthesis of histamine from histidine is catalyzed by the enzyme L-histidine decarboxylase. This homodimeric enzyme is a pyridoxal phosphate(PLP)-dependent decarboxylase and is highly specific for its histidine substrate. Ercan-Sencicek et al. noted that animal studies had shown that lack of Hdc in mice results in increased locomotor and stereotypic behaviors, as well as increased anxiety.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged proteins biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged proteins biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged proteins biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.

Description: It recognizes both the free and protein-conjugated (either soluble or cell bound) form of hexa-histidine. This MAb is highly specific to hexa-histidine and shows no cross-reaction with other structurally related compounds. It has a very high affinity for hexa-histidine and is excellent for use in various techniques. His-Tag Antibody detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein s biochemical properties. A variety of plasmids contain DNA that encodes an amino-terminal tag consisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography. As is the case with other protein tag systems, this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest.