Recombinant Human Aminoacylase-1(ACY1) CSB-EP860799HU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
N-acyl-L-amino-acid amidohydrolase
Species: (Organism)
Homo sapiens (Human)
Gene Names:
ACY1
Tag info:
N-terminal GST-tagged
Target Protein AA Sequence:
MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALASVPALPSDS
Expression Region:
1-408aa
Subcellular Location:
Cytoplasm
Tissue Specificity:
Expression is highest in kidney, strong in brain and weaker in placenta and spleen.
Protein Length:
Full Length
Pathway:
Mol. Weight:
72.9 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Signal Transduction
Function:
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Involvement in disease:
Aminoacylase-1 deficiency (ACY1D)
Relevance:
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Peptidase M20A family
Reference:
"The nucleotide sequence of human aminoacylase-1." Mitta M., Kato I., Tsunasawa S. Biochim. Biophys. Acta 1174:201-203(1993)
