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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

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
MFCD00162530
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
DB, ELISA (d), IHC (p)
Citations:
16

Key Documents

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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

200

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.

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)

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.

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GHS07

signalword

Warning

hcodes

H317

Hazard Classifications

Skin Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

A5175-BULK: + A5175-VAR: + A5175-1ML:4548173186191

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Certificates of Analysis (COA)

Lot/Batch Number
0000512466
0000493835
0000493835
0000419997
0000397131

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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)
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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