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B0271

Sigma-Aldrich

Monoclonal Anti-β-Galactosidase−Biotin Conjugate antibody produced in mouse

clone GAL-13, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Monoclonal Anti-β-Galactosidase

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

conjugate

biotin conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

GAL-13, monoclonal

form

buffered aqueous solution

species reactivity

bacteria

technique(s)

dot blot: 1:2,000

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Monoclonal Anti-b-Galactosidase (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. ß-Galactosidase enzyme is encoded by lacZ gene of E. coli.

Specificity

The antibody may be used for amplification in immunoenzymatic staining by preparing a β-galactosidase anti-β-galactosidase (BGABG) soluble complex. It is not recommended for immunoblotting; it does not recognize denatured or reduced β-galactosidase.

Immunogen

β-galactosidase from E. coli

Application

Monoclonal Anti-β-Galactosidase-Biotin Conjugate antibody produced in mouse may be used with ExtrAvidin-Peroxidase in the dot blot technique on native, purified, or crude β-galactosidase. The antibody was used to detect β-galactosidase by immunofluorescence in paraffin-embedded adult mouse kidney sections. It was used in ELISPOT assays at a dilution of 1:1000.

Biochem/physiol Actions

β-galactosidase enzyme is encoded by lacZ gene of E. coli; it acts on lactose and cleaves it to glucose and galactose. Monoclonal Anti-β-Galactosidase-Biotin Conjugate antibody binds with soluble enzyme even when bound to a surface without causing any loss of enzymatic activity. It is used as readout for promoter activity in lacZ transfected cells.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

Preparation Note

Prepared by conjugation with ε-aminocaproyl biotin.

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 Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Jennifer E Snyder-Cappione et al.
Journal of immunology (Baltimore, Md. : 1950), 176(4), 2662-2668 (2006-02-04)
CD8(+) T cells in HIV-infected patients are believed to contribute to the containment of the virus and the delay of disease progression. However, the frequencies of HIV-specific CD8(+) T cells, as measured by IFN-gamma secretion and tetramer binding, often do
U Rüther et al.
The EMBO journal, 2(10), 1791-1794 (1983-01-01)
A set of six cloning vectors, pUR 278, 288, 289, 290, 291, 292 is presented. These vectors have the cloning sites, BamHI, SalI, PstI, XbaI and HindIII, in all frames at the 3' end of the lacZ gene. Insertion of
A Roth et al.
The EMBO journal, 14(9), 2106-2111 (1995-05-01)
The 94 C-terminal amino acids of the initiator protein DnaA of Escherichia coli are required and sufficient for specific binding to the cognate DNA binding site. The binding domain contains two potential amphipathic alpha-helices and a third alpha-helix. It represents
G M Weinstock et al.
Proceedings of the National Academy of Sciences of the United States of America, 80(14), 4432-4436 (1983-07-01)
We have developed an Escherichia coli plasmid vector for the identification and expression of foreign DNA segments that are open reading frames (ORFs). The 5' end of ompF, an E. coli gene encoding an abundant outer membrane protein, is used
Benjamin D Humphreys et al.
The American journal of pathology, 176(1), 85-97 (2009-12-17)
Understanding the origin of myofibroblasts in kidney is of great interest because these cells are responsible for scar formation in fibrotic kidney disease. Recent studies suggest epithelial cells are an important source of myofibroblasts through a process described as the
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