Human Aldehyde Dehydrogenase 4 Family, Member A1 (ALDH4A1) Protein

Este producto es parte de ALDH - Aldehyde dehydrogenase family member
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1495€ (100 µg)

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935106861
info@markelab.com
name
Human Aldehyde Dehydrogenase 4 Family, Member A1 (ALDH4A1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx693708
tested applications
SDS-PAGE

Description

Human ALDH4A1 Protein is a recombinant protein from Human produced in Baculovirus-Insect Cells. A DNA sequence encoding the human ALDH4A1 (AAH07581.1) (Lys 25-Gln 563) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.

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Product specifications

CategoryProteins and Peptides
Immunogen TargetALDH4A1
HostInsect
OriginHuman
Observed MWMolecular Weight: 59.2 kDa Sequence Fragment: Lys25-Gln563 Validity: The validity for this protein is 12 months.
ExpressionRecombinant
Purity> 95% (SDS-PAGE)
Size 1100 µg
Form
Tested ApplicationsSDS-PAGE
BufferLyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 8.5.
AvailabilityShipped within 5-15 working days.
StorageAliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles.
Dry IceNo
NCBI AccessionAAH07581.1
AliasP5C dehydrogenase
BackgroundProtein ALDH4A1
StatusRUO
NoteThis product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

ALDH4A1, also known as pyrroline-5-carboxylate dehydrogenase (P5CDH), is a mitochondrial enzyme that catalyzes the conversion of pyrroline-5-carboxylate (P5C) into glutamate as part of the proline degradation pathway. This reaction is critical for maintaining amino acid metabolism, nitrogen balance, and cellular energy production. ALDH4A1 is expressed in tissues such as the liver, kidneys, and muscles, where proline serves as a key energy substrate. Mutations in ALDH4A1 lead to hyperprolinemia type II, a rare metabolic disorder characterized by elevated levels of proline and P5C, causing neurological symptoms, seizures, and cognitive impairments. ALDH4A1 also plays a role in protecting cells from oxidative stress, as proline metabolism generates NADH, which supports mitochondrial function. Its regulation is critical for amino acid catabolism, energy balance, and stress responses under nutrient deprivation.

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