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A7164

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Synonym(s):

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

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About This Item

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

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: 1:1,000

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... IGK@(50802)

General description

Human κ light chains are antibody fragments that regulate immunological responses in cells. Increased expression of κ light chains has been linked to chronic lymphocytic leukemia . The variable fragment of the κ light chain gene has also been associated with vaccine-induced antibody response to the polysaccharide coat in Haemophilus influenzae type b . Anti-Human κ Light Chains (Bound and Free)-Peroxidase antibody detects human κ (bound and free) light chains when tested against human IgA, IgG, IgM, and Bence Jones κ and λ myeloma proteins.

Immunogen

Purified human κ light chains

Application

Anti-Human κ Light Chains (Bound and Free)-Peroxidase antibody is suitable for use in western blot (1:1000).
ELISA Assays were performed using HRP-conjugated goat anti-human kappa light chains IgG to detect IgG1 and free K chains in cultured media of human LCL cells.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4 containing 1% bovine serum albumin with preservative.

Preparation Note

Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, p215, (Elsevier/North Holland Biomedical Press, Amsterdam, 1978).

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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Pictograms

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Signal Word

Warning

Hazard Statements

Hazard Classifications

Aquatic Chronic 2 - Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Lin Zhang et al.
Bioconjugate chemistry, 32(6), 1094-1104 (2021-05-21)
Antibody-drug conjugates (ADCs) are complex pharmaceutical molecules that combine monoclonal antibodies with biologically active drugs through chemical linkers. ADCs are designed to specifically kill disease cells by utilizing the target specificity of antibodies and the cytotoxicity of chemical drugs. However
Mélanie Chypre et al.
Immunology letters, 171, 5-14 (2016-01-17)
Antibodies play an important role in therapy and investigative biomedical research. The TNF-family member Receptor Activator of NF-κB (RANK) is known for its role in bone homeostasis and is increasingly recognized as a central player in immune regulation and epithelial
Christina L Parker et al.
mBio, 11(1) (2020-01-23)
Despite their exceptional potencies, the broad tropism of most commonly used lentivirus (LV) vectors limits their use for targeted gene delivery in vivo We hypothesized that we could improve the specificity of LV targeting by coupling (i) reduction of their
Laura Montero-Morales et al.
Frontiers in bioengineering and biotechnology, 7, 242-242 (2019-10-22)
Human immunoglobulin E (IgE) is the most extensively glycosylated antibody isotype so glycans attached to the seven N-glycosites (NGS) in its Fab and Fc domains may modulate its functions. However, targeted modification of glycans in multiply glycosylated proteins remains a
Nicolas Boute et al.
Frontiers in pharmacology, 7, 27-27 (2016-03-01)
Based on the recent development of NanoLuc luciferase (Nluc), a small (19 kDa), highly stable, ATP independent, bioluminescent protein, an extremely robust and ultra high sensitivity screening system has been developed whereby primary hits of therapeutic antibodies and antibody fragments

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