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Key Documents

06-719

Sigma-Aldrich

Anti-LexA Antibody, DNA-binding region

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

E. coli

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

Escherichia coli K12 ... Lexa(948544)

General description

The anti-LexA Antibody allows detection of LexA protein and recombinant proteins fused to the LexA protein. This antibody can be used to detect expression of potential bait proteins constructed for use with the yeast two-hybrid system or other interaction trap systems. LexA adds about 22 to 25 kDa to your protein, depending on the number of extra amino acids.

Specificity

Recognizes LexA portion of bait fusion proteins used in the yeast two-hybrid system.

Immunogen

His-tagged DNA binding domain of LexA protein corresponding to amino acid residues 1-202

Application

Detect LexA with Anti-LexA Antibody, DNA-binding region (Rabbit Polyclonal Antibody), that has been shown to work in IP & WB.

Quality

routinely evaluated by immunoblot on LexA-pRB transfected yeast lysate

Target description

24 kDa

Physical form

Format: Purified

Analysis Note

Control
LexA-pRB transfected yeast cell extract

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Tyrosine residues direct the ubiquitination and degradation of the NY-1 hantavirus G1 cytoplasmic tail.
Erika Geimonen, Imelyn Fernandez, Irina N Gavrilovskaya, Erich R Mackow
Journal of virology null
Seiji Tanaka
Genes to cells : devoted to molecular & cellular mechanisms, 24(12), 781-788 (2019-10-11)
Protein-protein interactions are one of the most basic and critical processes underlying biological functions. Thus, identification of the interacting proteins of a protein of interest and further elucidation of the roles of the interactions is critical for understanding the related
The SOS regulatory system of Escherichia coli.
Little, J W and Mount, D W
Cell, 29, 11-22 (1982)
Genome-wide analysis of the functions of a conserved surface on the corepressor Tup1.
Green, SR; Johnson, AD
Molecular Biology of the Cell null
Notch signaling is antagonized by SAO-1, a novel GYF-domain protein that interacts with the E3 ubiquitin ligase SEL-10 in Caenorhabditis elegans.
Hale, VA; Guiney, EL; Goldberg, LY; Haduong, JH; Kwartler, CS; Scangos, KW; Goutte, C
Genetics null

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