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Key Documents

SAB1300633

Sigma-Aldrich

Anti-PDX1 (N-term) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-E3-binding protein, Anti-Pyruvate dehydrogenase protein X component, Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

immunohistochemistry: 1:50-1:100
indirect ELISA: 1:1000

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PDX1(8050)

General description

PDX1, located in the mitochondrial matrix, is required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by noncovalent bonds. Defects in PDHX are a cause of lacticacidemia. PDX1 belongs to the 2-oxoacid dehydrogenase family and contains 1 lipoyl-binding domain.

Immunogen

PDX1 (9-40)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human PDX1.

Physical form

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.

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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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W Lu et al.
European review for medical and pharmacological sciences, 18(7), 941-948 (2014-04-26)
This study aimed to observe the influence of intermittent hypoxia on rat INS-1 cells and the protective effect of melatonin (MT). Intermittent hypoxia condition was induced in rat INS-1 cells. The supernatants were used to detect oxidative stress indicators, and

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