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A5062

Sigma-Aldrich

Anti-Guinea Pig IgG (whole molecule)−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

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About This Item

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

biological source

goat

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

technique(s)

direct ELISA: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

General description

Immunoglobulin G (IgG) is a glycoprotein antibody that regulates immune responses such as phagocytosis and is also involved in the development of autoimmune diseases . In guinea pig IgG is subdivided into-IgG1 and IgG2. IgG2 can bind to Fc receptor of macrophages and monocytes. Anti-guinea pig IgG (whole molecule) −alkaline phosphatase antibody can be used in immunohistology (diluted 1:50). Goat anti-guinea pig IgG (whole molecule) −alkaline phosphatase antibody reacts specifically with guinea pig IgG.

Immunogen

Purified guinea pig IgG.

Application

Anti-guinea pig IgG (whole molecule) −alkaline phosphatase antibody can be used in direct ELISA (diluted 1:30,000) and dot blot.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western blot analysis of SF9 cells was performed using alkaline phosphatase conjugated goat anti-guinea pig IgGat 1:10000 as the secondary.

Physical form

Solution in 0.05 M Tris, pH 8.0, containing 1 mM MgCl2, 10 mM glycine, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide

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

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Anahita Daryabeigi et al.
Genetics, 203(2), 733-748 (2016-04-22)
SUN (Sad1 and UNC-84) and KASH (Klarsicht, ANC-1, and Syne homology) proteins are constituents of the inner and outer nuclear membranes. They interact in the perinuclear space via C-terminal SUN-KASH domains to form the linker of nucleoskeleton and cytoskeleton (LINC)
Philippe P Pagni et al.
Diabetes, 63(6), 2015-2025 (2014-02-13)
Type 1 diabetes is thought to be an autoimmune condition in which self-reactive T cells attack insulin-secreting pancreatic β-cells. As a proinflammatory cytokine produced by β-cells or macrophages, interleukin-1β (IL-1β) represents a potential therapeutic target in diabetes. We reasoned IL-1β
K Schønning et al.
Journal of virology, 73(10), 8364-8370 (1999-09-11)
In order to study the stoichiometry of monoclonal antibody (MAb) neutralization of T-cell line-adapted human immunodeficiency virus type 1 (HIV-1) in antibody excess and under equilibrium conditions, we exploited the ability of HIV-1 to generate mixed oligomers when different env
M D Alexander et al.
Immunology, 35(1), 115-123 (1978-07-01)
Guinea-pig IgG2 and IgT1 bind to contiguous Fc receptors on homologous peritoneal macrophages. Equilibrium association constants determined for the binding of human IgG subclasses to homologous peripheral blood monocytes show that the order of binding is IgG1 greater than IgG3
Jens Modrof et al.
Journal of virology, 79(15), 10023-10031 (2005-07-15)
In bluetongue virus (BTV)-infected cells, large cytoplasmic aggregates are formed, termed viral inclusion bodies (VIBs), which are believed to be the sites of viral replication and morphogenesis. The BTV nonstructural protein NS2 is the major component of VIBs. NS2 undergoes

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