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
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
biological source
goat
Quality Level
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
Related Categories
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.
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)
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
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.
Not finding the right product?
Try our Product Selector Tool.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Raffaele Lombardi et al.
Transgenic research, 19(6), 1083-1097 (2010-03-17)
It was previously demonstrated that the tumour-targeting antibody mAb H10 can be transiently expressed and purified at high levels in Nicotiana benthamiana by using a vacuum-agroinfiltration system boosted by the use of a virus silencing suppressor protein. Scope of this
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
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)
Efficient Agrobacterium-based transient expression system for the production of biopharmaceuticals in plants
Circelli P, et al.
Bioengineered Bugs, 1, 221-224 (2010)
Cristina Capodicasa et al.
Biotechnology and bioengineering, 114(12), 2729-2738 (2017-08-24)
Immunoglobulins A (IgA) are crucially involved in protection of human mucosal surfaces from microbial pathogens. In this work, we devised and expressed in plants recombinant chimeric antifungal antibodies (Abs) of isotype A (IgA1, IgA2, and scFvFcA1), derived from a murine
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service