Recombinant Human GLUD2, GST-tagged

• Cat.No.: GLUD2-13320H
• Product Overview: Recombinant Human GLUD2 protein, fused to GST-tag, was expressed in E.coli and purified by GSH-sepharose.

Specification

• Species: Human
• Source: E.coli
• Tag: GST
• Protein Length: 207-558a.a.
• Description: The protein encoded by this gene belongs to the glucagon family and is a preproprotein that is produced in the hypothalamus. The preproprotein is cleaved to form a 44 aa factor, also called somatocrinin, that acts to stimulate growth hormone release from the pituitary. Variant receptors for somatocrinin have been found in several types of tumors, and antagonists of these receptors can inhibit the growth of the tumors. Defects in this gene are a cause of dwarfism, while hypersecretion of the encoded protein is a cause of gigantism.
• Storage: The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles.
• Storage Buffer: 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 100mM GSH and 1% Triton X-100,15%glycerol.

Gene Information

• Gene Name: GLUD2 glutamate dehydrogenase 2 [ Homo sapiens ]
• Official Symbol: GLUD2
• Synonyms: GLUD2; glutamate dehydrogenase 2; GLUDP1, glutamate dehydrogenase pseudogene 1; glutamate dehydrogenase 2, mitochondrial; GDH 2; glutamate dehydrogenase pseudogene 1; GDH2; GLUDP1
• Gene ID: 2747
• mRNA Refseq: NM_012084
• Protein Refseq: NP_036216
• MIM: 300144
• UniProt ID: P49448
• Chromosome Location: Xq24-q25
• Pathway: Alanine, aspartate and glutamate metabolism, organism-specific biosystem; Alanine, aspartate and glutamate metabolism, conserved biosystem; Arginine and proline metabolism, organism-specific biosystem; Arginine and proline metabolism, conserved biosystem; D-Glutamine and D-glutamate metabolism, organism-specific biosystem; D-Glutamine and D-glutamate metabolism, conserved biosystem; Metabolic pathways, organism-specific biosystem
• Function: ADP binding; GTP binding; glutamate dehydrogenase (NAD+) activity; glutamate dehydrogenase [NAD(P)+] activity; leucine binding; nucleotide binding; oxidoreductase activity