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Merck

A5175

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Sinónimos:

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

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.46

origen biológico

goat

Nivel de calidad

conjugado

peroxidase conjugate

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

secondary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

técnicas

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

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Descripción general

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.

Aplicación

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)

Forma física

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

Nota de preparación

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

Información legal

Ampliflu is a trademark of Sigma-Aldrich Co. LLC

Cláusula de descargo de responsabilidad

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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Pictogramas

Exclamation mark

Palabra de señalización

Warning

Frases de peligro

Clasificaciones de peligro

Skin Sens. 1

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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
Verena K Hehle et al.
Plant biotechnology journal, 13(2), 235-245 (2014-10-07)
Plants are promising hosts for the production of monoclonal antibodies (mAbs). However, proteolytic degradation of antibodies produced both in stable transgenic plants and using transient expression systems is still a major issue for efficient high-yield recombinant protein accumulation. In this

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