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Key Documents

A5175

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

동의어(들):

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

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.46

생물학적 소스

goat

결합

peroxidase conjugate

항체 형태

affinity isolated antibody

항체 생산 유형

secondary antibodies

클론

polyclonal

형태

buffered aqueous solution

기술

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

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

관련 카테고리

일반 설명

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.

애플리케이션

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)

물리적 형태

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

제조 메모

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

법적 정보

Ampliflu is a trademark of Sigma-Aldrich Co. LLC

면책조항

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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픽토그램

Exclamation mark

신호어

Warning

유해 및 위험 성명서

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


시험 성적서(COA)

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문서 라이브러리 방문

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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