LIAS Antibody (C-Term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, E |
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Primary Accession | O43766 |
Other Accession | Q5BIP7, Q6GQ48 |
Reactivity | Human, Rat, Mouse |
Predicted | Bovine |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 41911 Da |
Gene ID | 11019 |
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Other Names | Lipoyl synthase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03123}, 2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03123}, Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03123}, LS {ECO:0000255|HAMAP-Rule:MF_03123}, Lip-syn {ECO:0000255|HAMAP-Rule:MF_03123}, Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03123}, LIAS {ECO:0000255|HAMAP-Rule:MF_03123}, LAS |
Target/Specificity | This LIAS antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 298-330 amino acids from human LIAS. |
Dilution | WB~~1:2000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | LIAS Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | LIAS {ECO:0000255|HAMAP-Rule:MF_03123} |
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Synonyms | LAS |
Function | 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. |
Cellular Location | Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123}. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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.
REFERENCES
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Hillier L.W.,et al.Nature 434:724-731(2005).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Stanchi F.,et al.Yeast 18:69-80(2001).
Mayr J.A.,et al.Am. J. Hum. Genet. 89:792-797(2011).

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