Mouse Aminoacylase-1 (ACY1) Protein (Active)
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Description
Aminoacylase-1 (ACY1) protein is a recombinant Mouse protein expressed in HEK293 cells.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Aminoacylase-1 (ACY1) |
| Host | HEK293 cells |
| Assay Type | Activity: Active Sequence Fragment: Met1-Ser408 Tag: C-terminal His tag |
| Origin | Mouse |
| Observed MW | 45 kDa |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 50 µg |
| Form | Lyophilized |
| Tested Applications | SDS-PAGE |
| Buffer | Prior to lyophilization: Sterile PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Storage: Store lyophilized between -20 °C and -80°C. Stability: Stable when stored reconstituted at 2-8°C for up to 1 week. Reconstituted aliquots are stable at -20°C for up to 3 months. Shelf Life: 12 months. |
| Dry Ice | No |
| UniProt ID | Q99JW2 |
| Alias | N-acyl-L-amino-acid amidohydrolase,ACY-1 |
| Background | Protein ACY1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. Endotoxin Level: < 1.0 EU per µg (LAL method). |
Descripción
ACY1 is a cytosolic enzyme responsible for catalyzing the hydrolysis of N-acylated amino acids into free amino acids and their corresponding acyl groups. This process is crucial for the metabolism and recycling of amino acids, particularly in tissues like the liver and kidneys, where ACY1 contributes to nitrogen balance and detoxification. ACY1 plays a role in regulating the intracellular pool of amino acids for protein synthesis and metabolic processes. Deficiency in ACY1 activity, caused by genetic mutations, leads to aminoacylase 1 deficiency, a rare metabolic disorder characterized by the accumulation of N-acetylated amino acids in the urine, with possible neurological and developmental consequences. In addition to its metabolic role, ACY1 is expressed in certain cancers, where it may influence tumor metabolism and growth. Its enzymatic function in amino acid metabolism underscores its importance in cellular and systemic homeostasis.
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This gene encodes a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and an acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. This gene is located on chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and this enzyme is the first member of a new family of zinc-binding enzymes. Mutations in this gene cause aminoacylase-1 deficiency, a metabolic disorder characterized by central nervous system defects and increased urinary excretion of N-acetylated amino acids. Alternative splicing of this gene results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream ABHD14A (abhydrolase domain containing 14A) gene, as represented in GeneID:100526760. A related pseudogene has been identified on chromosome 18.
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