A5175
Anti-Human Lambda Light Chains (Bound and Free)−Peroxidase antibody produced in goat
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Goat Anti-Human Lambda Light Chains (Bound and Free)-HRP
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About This Item
Product Name
Anti-Human Lambda Light Chains (Bound and Free)−Peroxidase antibody produced in goat, affinity isolated antibody, buffered aqueous solution
biological source
goat
conjugate
peroxidase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
technique(s)
direct ELISA: 1:35,000
dot blot: 1:40,000 (chemiluminescent)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Related Categories
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)
Enzyme-linked immunosorbent assay (1 paper)
Western Blotting (1 paper)
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.
General description
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.
Preparation Note
Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
Legal Information
Ampliflu is a trademark of Sigma-Aldrich Co. LLC
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Warning
hcodes
Hazard Classifications
Skin Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Efficient Agrobacterium-based transient expression system for the production of biopharmaceuticals in plants
Circelli P, et al.
Bioengineered Bugs, 1, 221-224 (2010)
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
Philippe V Jutras et al.
PloS one, 11(11), e0167086-e0167086 (2016-11-29)
The overall quality of recombinant IgG antibodies in plants is dramatically compromised by host endogenous proteases. Different approaches have been developed to reduce the impact of endogenous proteolysis on IgGs, notably involving site-directed mutagenesis to eliminate protease-susceptible sites or the
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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