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Recombinant Human Lipoyl synthase, mitochondrial (LIAS)

Recombinant Human Lipoyl synthase, mitochondrial (LIAS)

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

LIAS

Uniprot NO.

O43766

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

28-372

Target Protein Sequence

LSS LPDKKKELLQ NGPDLQDFVS GDLADRSTWD EYKGNLKRQK GERLRLPPWL KTEIPMGKNY NKLKNTLRNL NLHTVCEEAR CPNIGECWGG GEYATATATI MLMGDTCTRG CRFCSVKTAR NPPPLDASEP YNTAKAIAEW GLDYVVLTSV DRDDMPDGGA EHIAKTVSYL KERNPKILVE CLTPDFRGDL KAIEKVALSG LDVYAHNVET VPELQSKVRD PRANFDQSLR VLKHAKKVQP DVISKTSIML GLGENDEQVY ATMKALREAD VDCLTLGQYM QPTRRHLKVE EYITPEKFKY WEKVGNELGF HYTASGPLVR SSYKAGEFFL KNLVAKRKTK DL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.

Gene References into Functions

this study used a bioinformatics approach to predict its structure. . A homology model for LIAS protein was generated using X-ray crystallographic structure of Thermosynechococcus elogatsu. The active site of LIAS protein was mapped and docked with S-Adenosyl Methionine PMID:27717843
oxoglutarate dehydrogenase (OGDH) and lipoic acid synthase (LIAS), which when mutated stabilize HIF1alpha in a non-hydroxylated form. PMID:27923773
heterozygous mutations (c.738-2A>G and c.929T>C (p.Met310Thr)) in LIAS. PMID:26108146
Patients with LIAS nonketotic hyperglycinemia varied in disease severity and cortical involvement. PMID:24334290
We identified the homozygous mutation c.746G>A (p.Arg249His) in LIAS in an individual with neonatal-onset epilepsy, muscular hypotonia, lactic acidosis, and elevated glycine concentration in plasma and urine PMID:22152680
Lipoic acid synthetase deficiency results in an overall disturbance in the antioxidant defense network, leading to increased inflammation, insulin resistance, and mitochondrial dysfunction. PMID:19074983