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R5506

Sigma-Aldrich

Anti-Rabbit IgG (whole molecule) antibody produced in goat

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Rabbit IgG Antibody

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About This Item

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

biological source

goat

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

indirect ELISA: 1:30,000
quantitative precipitin assay: 3.0-4.5 mg/mL

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Immunoglobulins (Igs) belong to the immunoglobulin super-family and have two heavy (H) and two light (L) chains, held together by disulfide linkages. The heavy chain has one variable N-terminal region and three to four constant (CH1-CH4) C-terminal regions. The L chain comprises of one variable N-terminal region and a constant C-terminal region. IgG is an abundant protein in human serum. The four classes of IgG include IgG1, IgG2, IgG3 and IgG4. The IgG heavy chain region is mapped to human chromosome 14.
Rabbit immunoglobulins (IgGs) are often used as primary antibodies in several protein assays. Thus, anti-rabbit IgGs can be used as secondary antibodies to study and characterize target proteins bound to rabbit IgGs. Anti-Rabbit IgG (whole molecule) antibody is specific for IgGs in rabbits.

Specificity

Anti-Rabbit IgG (whole molecule) antibody is specific for IgGs in rabbits.

Immunogen

Rabbit IgG

Application

Anti-Rabbit IgG (whole molecule) antibody is suitable for use in quantitative precipitin assay, immunoelectrophoresis, immunohistochemistry , and laser scattering microscopy .
Anti-Rabbit IgG (whole molecule) antibody produced in goat has been used as secondary antibody in vivo xenograft assay in non-small-cell lung cancer (NSCLC) tissues and in western blotting detection in endometrial sample from cattle.

Biochem/physiol Actions

Digestion of IgG by papain results in the generation of fragment antigen binding (Fab). Pepsin digestion of IgG produces fragment crystallizable (Fc). The Fc region of IgG antibody has enormous therapeutic potential and is exploited for the development of therapeutic antibodies. IgG1 class is the most abundant and its deficiency results in hypogammaglobulinemia. IgG2 deficiency increases susceptibility to bacterial infections. IgG3 mediates effector functions, and IgG4 is associated with asymptomatic infection.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as preservative

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing, or storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

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


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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E F Kirkness et al.
The Biochemical journal, 256(1), 291-294 (1988-11-15)
A synthetic peptide, corresponding to amino acid residues 101-109 of the bovine gamma-aminobutyrate/benzodiazepine receptor alpha-subunit, was used to raise a polyclonal antiserum. The reactivity of this antiserum towards polypeptides of both bovine and pig receptor preparations was established by immunoprecipitation
J Yuan et al.
Experimental mechanics, 50(9) (2010-11-01)
At room temperature at stall, the flagellar motor of the bacterium Escherichia coli exerts a torque of ~1300 pN nm. At zero external load, it spins ~330 Hz. A robust method for studying the motor near zero load is reviewed
Junhua Yuan et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(4), 1182-1185 (2008-01-19)
Flagellated bacteria, such as Escherichia coli, are propelled by helical flagellar filaments, each driven at its base by a reversible rotary motor, powered by a transmembrane proton flux. Torque is generated by the interaction of stator proteins, MotA and MotB
MicroRNA-30a suppresses non-small-cell lung cancer by targeting Myb-related protein B.
Geng GJ, et al.
Experimental and Therapeutic Medicine, 15(2), 1633-1639 (2018)
Steven Johnson et al.
Nature microbiology, 6(6), 712-721 (2021-05-02)
The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the inner membrane to the micrometre-long flagellar filament that powers bacterial swimming in viscous

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