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Merck
CN

06-719

Anti-LexA Antibody, DNA-binding region

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IP, WB
Citations:
31

Key Documents

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biological source

rabbit

conjugate

unconjugated

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.

NP_418467.1

UniProt accession no.

P0A7C2

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

100

Gene Information

Escherichia coli K12 ... Lexa(948544)

General description

24 kDa
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.

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.

Biochem/physiol Actions

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

Physical form

Format: Purified

Analysis Note

Control
LexA-pRB transfected yeast cell extract
routinely evaluated by immunoblot on LexA-pRB transfected yeast lysate

Legal Information

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

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Storage Class

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
The SOS regulatory system of Escherichia coli.
Little, J W and Mount, D W
Cell, 29, 11-22 (1982)
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
Yu-Fan Chen et al.
Molecular and cellular biology, 36(15), 2039-2050 (2016-05-18)
Cohesin associates with distinct sites on chromosomes to mediate sister chromatid cohesion. Single cohesin complexes are thought to bind by encircling both sister chromatids in a topological embrace. Transcriptionally repressed chromosomal domains in the yeast Saccharomyces cerevisiae represent specialized sites
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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