Ugrás a tartalomra
Merck

A2909

Sigma-Aldrich

Rabbit IgG−Agarose

saline suspension

Szinonimák:

IgG agarose beads

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.46

konjugátum

agarose conjugate

Minőségi szint

form

saline suspension

a címkézés mértéke

≥5 mg per mL

technika/technikák

immunoprecipitation (IP): suitable

matrix

cross-linked 4% beaded agarose

mátrix aktiválás

cyanogen bromide

mátrix távtartó

1 atom

tárolási hőmérséklet

2-8°C

Általános leírás

IgGs are glycoprotein antibodies that modulate several immune responses. IgG-Agarose is an immunoadsorbent that can be used to purify antibodies, remove species specific cross-reacting antibodies, or remove contaminating antibodies from an antiserum preparation. Characteristically, cross-reacting antibodies may be removed from an antiserum preparation using an equal resin volume of IgG-Agarose. However, the resin to antiserum ratio will vary with individual applications. Immunoglobulin G (IgG) is part of the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50 kDa and 25 kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively.

Alkalmazás

Rabbit IgG antibody (20 μl/ml) crosslinked to agarose beads was used to isolate RAT tagged proteins from whole cell extracts of 293T cells.Rabbit IgG crosslinked to agarose beads were used for purification of tagged protein from mammalian whole cell extracts at 0.5 to 1.0mg total protein to 10 μl of beads.
Rabbit IgG-Agarose has been used for immunoprecipitation and affinity purification assays.

Fizikai forma

suspension in 0.5 M NaCl containing preservative.

Jogi nyilatkozat

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.

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 3


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Dokumentumtár megtekintése

David Atencio et al.
G3 (Bethesda, Md.), 4(3), 523-537 (2014-01-29)
The Ess1 prolyl isomerase from Saccharomyces cerevisiae and its human ortholog, Pin1, play critical roles in transcription by regulating RNA polymerase II. In human cells, Pin1 also regulates a variety of signaling proteins, and Pin1 misexpression is linked to several
D L Lafontaine et al.
Genes & development, 12(4), 527-537 (1998-03-21)
Many or all of the sites of pseudouridine (Psi) formation in eukaryotic rRNA are selected by site-specific base-pairing with members of the box H + ACA class of small nucleolar RNAs (snoRNAs). Database searches previously identified strong homology between the
Antibody structure, instability, and formulation
Wang W, et al.
Journal of Pharmaceutical Sciences (2007)
Guixin Du et al.
PloS one, 8(12), e81583-e81583 (2013-12-21)
Human cytomegalovirus protein IE2-p86 exerts its functions through interaction with other viral and cellular proteins. To further delineate its protein interaction network, we generated a recombinant virus expressing SG-tagged IE2-p86 and used tandem affinity purification coupled with mass spectrometry. A
Alison L Pidoux et al.
Molecular cell, 33(3), 299-311 (2009-02-17)
The mechanisms ensuring specific incorporation of CENP-A at centromeres are poorly understood. Mis16 and Mis18 are required for CENP-A localization at centromeres and form a complex that is conserved from fission yeast to human. Fission yeast sim1 mutants that alleviate

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