Description : |
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. |
Source : |
HEK293 |
Species : |
Human |
Tag : |
Myc/DDK |
Molecular Mass : |
45.9 kDa |
AA Sequence : |
MTSKGPEEEHPSVTLFRQYLRIRTV QPKPDYGAAVAFFEETARQLGLGCQ KVEVAPGYVVTVLTWPGTNPTLSSI LLNSHTDVVPVFKEHWSHDPFEAFK DSEGYIYARGAQDMKCVSIQYLEAV RRLKVEGHRFPRTIHMTFVPDEEVG GHQGMELFVQRPEFHALRAGFALDE GIANPTDAFTVFYSERSPWWVRVTS TGRPGHASRFMEDTAAEKLHKVVNS ILAFREKEWQRLQSNPHLKEGSVTS VNLTKLEGGVAYNVIPATMSASFDF RVAPDVDFKAFEEQLQSWCQAAGEG VTLEFAQKWMHPQVTPTDDSNPWWA AFSRVCKDMNLTLEPEIMPAATDNR YIRAVGVPALGFSPMNRTPVLLHDH DERLHEAVFLRGVDIYTRLLPALAS VPALPSDSTRTRPLEQKLISEEDLA ANDILDYKDDDDKV |
Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : |
Stable for 3 months from receipt of products under proper storage and handling conditions. |
Storage : |
Store at -80 centigrade. Avoid repeated freeze-thaw cycles. |
Concentration : |
50 μg/mL as determined by BCA |
Storage Buffer : |
100 mM glycine, 25 mM Tris-HCl, pH 7.3. |