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Key Documents

A4174

Sigma-Aldrich

Anti-Goat IgG (whole molecule)–Peroxidase antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Rabbit Anti-Goat IgG (whole molecule)–HRP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

Conjugué

peroxidase conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

goat

Ne doit pas réagir avec

human

Technique(s)

direct ELISA: 1:10,000

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Catégories apparentées

Description générale

IgG antibodies regulate several functions such as complement activation and phagocytosis. Thus they play a crucial role in facilitating cytological immune responses. Anti-goat IgG (whole molecule)–peroxidase antibody can be used as a secondary antibody in ovarian tissue microarray. Rabbit anti-goat IgG (whole molecule)-peroxidase antibody reacts specifically with all goat IgG but shows no reactivity with human serum proteins.

Immunogène

Purified goat IgG.

Application

Anti-Goat IgG (whole molecule)-Peroxidase antibody produced in rabbit is suitable for use in immunoblot and immunohistochemistry. The product can also be used for direct ELISA (1:10,000).
The presence of pleiotrophin in HUVEC cell culture medium was analyzed by western blot using HRP-conjugated rabbit anti-goat IgGas the secondary at a dilution of 1:7500 in TBST.

Autres remarques

Antibody adsorbed with human serum proteins.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 0.05% MIT.

Notes préparatoires

Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2


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Peter Horak et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 11(24 Pt 1), 8585-8591 (2005-12-20)
Epithelial ovarian cancer is the most common cause of mortality from gynecologic malignancies. Due to advanced stage at diagnosis, most patients need systemic treatment in addition to surgery. Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the
Johan Dixelius et al.
The Journal of biological chemistry, 279(22), 23766-23772 (2004-03-27)
Laminins are widely distributed extracellular matrix proteins. Certain laminin isoforms are predominant in vascular basement membranes and may be critical in maintaining the stability of the mature vessel. On the other hand, formation of new vessels during angiogenesis requires degradation
Harukiyo Kawamura et al.
Blood, 112(9), 3638-3649 (2008-07-31)
Vascular endothelial growth factor (VEGF)-A regulates vascular development and angiogenesis. VEGF isoforms differ in ability to bind coreceptors heparan sulfate (HS) and neuropilin-1 (NRP1). We used VEGF-A165 (which binds HS and NRP1), VEGF-A121 (binds neither HS nor NRP1), and parapoxvirus
Rebekka Mauser et al.
Epigenetics & chromatin, 10(1), 45-45 (2017-09-28)
Histone post-translational modifications (PTMs) play central roles in chromatin-templated processes. Combinations of two or more histone PTMs form unique interfaces for readout and recruitment of chromatin interacting complexes, but the genome-wide mapping of coexisting histone PTMs remains an experimentally difficult task.
Tomasz Klaus et al.
Frontiers in immunology, 9, 1096-1096 (2018-06-08)
Mouse IgG3 is highly protective against several life-threatening bacteria. This isotype is the only one among mouse IgGs that forms non-covalent oligomers, has increased functional affinity to polyvalent antigens, and efficiently agglutinates erythrocytes. IgG3 also triggers the complement cascade. The

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