Human Aminoacylase 1 (ACY1) Protein

Este producto es parte de ACY - Aminoacylase
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221€ (10 µg)

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935106861
info@markelab.com
name
Human Aminoacylase 1 (ACY1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx166619
tested applications
WB, SDS-PAGE

Description

Aminoacylase 1 Protein is a recombinant Human protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Immunogen Target
Aminoacylase 1 (ACY1)
Host
E. coli
Origin
Human
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 49.5 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Thr2-Ser408
Tag: N-terminal His tag
Expression
Recombinant
Purity
> 90%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-7 working days.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
Alias
N-acyl-L-amino-acid amidohydrolase,ACY-1
Background
Protein ACY1
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

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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ACY1 Antibody is a Rabbit Polyclonal antibody against ACY1. 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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