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A5175

Sigma-Aldrich

Anti-Human Lambda Light Chains (Bound and Free)−Peroxidase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Goat Anti-Human Lambda Light Chains (Bound and Free)-HRP

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About This Item

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

Source biologique

goat

Conjugué

peroxidase conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Technique(s)

direct ELISA: 1:35,000
dot blot: 1:40,000 (chemiluminescent)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

Mammalian antibodies contain one of two types of light chain, called kappa or lamba. Each chain contains a constant and a variable domain. Mammalian antibodies contain either two kappa or two lambda light chains.
Horseradish Peroxidase (HRP) is an enzyme that catalyzes the conversion of chromogenic substrates such as o-phenylenediamine (OPD), 4-chloro-1-naphthol 3,3′,5,5′-tetramethylbenzidine (TMB), 3,3′-Diaminobenzidine (DAB) or 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS); chemiluminescent substrates such as CPS-3 (enhanced luminal) and fluorogenic substrates such as Ampliflu Red into detectable chromophores, light-emitters or fluorescers, respectively.

Application

Anti-Human Lambda Light Chains (Bound and Free)?Peroxidase antibody produced in goat has been used in:
  • enzyme linked immunosorbent assay (ELISA)
  • immunohistology
  • dot blot
  • detecting and quantitating human lambda light chains (bound and free) via chromogenic, chemoluminescent or fluorogenic immunochemical or immunohistochemical techniques
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
Western Blotting (1 paper)

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.

Notes préparatoires

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

Informations légales

Ampliflu is a trademark of Sigma-Aldrich Co. LLC

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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Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Skin Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Sharad P Adekar et al.
Hybridoma (2005), 27(1), 11-17 (2008-02-26)
Monoclonal antibodies have demonstrated significant potential as therapeutics for botulinum neurotoxin exposures. We previously described a hybridoma method for cloning native human antibodies that uses a murine myeloma cell line that ectopically expresses the human telomerase catalytic subunit gene (hTERT)
Marcello Donini et al.
Bioengineered, 6(5), 299-302 (2015-07-18)
We have recently characterized the degradation profiles of 2 human IgG1 monoclonal antibodies, the tumor-targeting mAb H10 and the anti-HIV mAb 2G12. Both mAbs were produced in plants either as stable transgenics or using a transient expression system based on
Efficient Agrobacterium-based transient expression system for the production of biopharmaceuticals in plants
Circelli P, et al.
Bioengineered Bugs, 1, 221-224 (2010)
Anna Timofeeva et al.
Life (Basel, Switzerland), 12(2) (2022-02-26)
Though hundreds of thousands of papers are currently being published on HIV/AIDS, only tens of hundreds of them are devoted to the antibodies generated during the disease. Most of these papers discuss antibodies in HIV/AIDS as a diagnostic tool, and
Linda Schwaigerlehner et al.
Applied microbiology and biotechnology, 103(18), 7505-7518 (2019-07-28)
The production potential of recombinant monoclonal antibody (mAb) expressing cell lines depends, among other factors, on the intrinsic antibody structure determined by the amino acid sequence. In this study, we investigated the influence of somatic mutations in the V(D)J sequence

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