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MilliporeSigma

G6282

Sigma-Aldrich

Monoclonal Anti-β-Galactosidase antibody produced in mouse

clone GAL-40, ascites fluid

Sinónimos:

Mouse Anti-beta-Galactosidase

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

GAL-40, monoclonal

contains

15 mM sodium azide

species reactivity

bacteria

technique(s)

dot blot: suitable using soluble β-galactosidase
immunocytochemistry: suitable
western blot: 1:1,000 using denatured-reduced Escherichia coli β-galactosidase

isotype

IgM

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

β-Galactosidase is coded by the LacZ gene which helps to transform lactose into galactose.
β-galactosidase is a ~465 kDa tetrameric protein. Eukaryotic genes are usually cloned into E.coli β-galactosidase (lacZ) gene that results in a fusion hybrid of the desired gene product with the β-galactosidase enzyme . As the amount of the desired gene product in these cloned vector systems corresponds to the amount of β-galactosidase, enzyme assays for β-galactosidase can be utilized to detect the required gene product . Monoclonal anti-β-galactosidase antibodies are specific for β-galactosidase in E.coli and enable the analysis of β-galactosidase fusion proteins encoded by cloned vector systems.

Specificity

The antibody may be used for detection of β-galactosidase expressed by the E. coli lacZ gene encoded in many cloned gene sequences; serves as an indicator for fusion proteins encoded by an inserted DNA sequence.

Immunogen

β-D-galactosidase from E. coli

Application

Monoclonal Anti-β-Galactosidase antibody produced in mouse has been used for western blotting.
Monoclonal anti-β-galactosidase antibodies may be used in dot blot (using soluble β-galactosidase), western blot (at a dilution of 1:1,000, using denatured-reduced Escherichia coli β-galactosidase) and immunocytochemistry. This antibody may also be used for immunochemical assays such as ELISA, immunoblot and immunohistochemistry by using the stepwise procedure or by the preparation of β-galactosidase anti-β galactosidase (BBAG) complex. Additionally, this product is suitable for the detection and purification of recombinant fusion proteins encoded by cloning vectors containing the β-galactosidase gene. Monoclonal anti-β-galactosidase antibody is also used for the immunoenzymatic staining of bone marrow and blood smears, and tissue sections.

Biochem/physiol Actions

β-galactosidase catalyses the hydrolysis of lactose to form glucose and galactose. It serves as a reporter enzyme in a number of analysis such as studying the regulation of gene expression, protein function and structure determination, and examining of target gene expression. β-galactosidase is also known to yield coloured products by acting on several substrates. Thus, it is prefered as a reporter enzyme in applications involving gene expression regulation, analysis of protein function/structure, and target gene expression.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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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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J M Brackett et al.
Journal of immunological methods, 200(1-2), 39-46 (1997-01-15)
A rapid, specific, perfusion immunoassay for active anti-HBsAg monoclonal IgM is described. The immunoassay requires less than 3.5 min per sample. The precision was found to be 3.6% at an IgM concentration of 17 microg/ml. A detection limit of 1
Structure of ?-galactosidase at 3.2-? resolution obtained by cryo-electron microscopy
Bartesaghi A
Proceedings of the National Academy of Sciences of the USA, 111(32), 11709?11714-11709?11714 (2014)
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Biotechnology and bioengineering, 99(2), 261-267 (2007-07-13)
Many alternative strategies to immobilize and stabilize enzymes have been investigated in recent years for applications in biosensors. The entrapment of enzymes within silica-based nanospheres formed through silicification reactions provides high loading capacities for enzyme immobilization, resulting in high volumetric

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