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AB190760

Anti-Kappa light chain antibody [KLC264]

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(1 Publication)

Mouse Monoclonal IGKC antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human IGKV1D-16.

View Alternative Names

Immunoglobulin kappa constant, Ig kappa chain C region, Ig kappa chain C region AG, Ig kappa chain C region CUM, Ig kappa chain C region EU, Ig kappa chain C region OU, Ig kappa chain C region ROY, Ig kappa chain C region TI, IGKC

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Kappa light chain antibody [KLC264] (AB190760)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Kappa light chain antibody [KLC264] (AB190760)

Immunohistochemical analysis of paraffin-embedded Human tonsil tissue, labeling Kappa light chain using ab190760 at 1 μg/ml. Note cell membrane and cytoplasmic staining.

Western blot - Anti-Kappa light chain antibody [KLC264] (AB190760)
  • WB

Supplier Data

Western blot - Anti-Kappa light chain antibody [KLC264] (AB190760)

All lanes:

Western blot - Anti-Kappa light chain antibody [KLC264] (ab190760) at 2 µg/mL

All lanes:

Human spleen tissue lysate

Predicted band size: 25 kDa,76 kDa

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

KLC264

Isotype

IgG1

Light chain type

kappa

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human IGKV1D-16.

P01601

Specificity

This antibody is specific to kappa light chain of immunoglobulin and shows no cross-reaction with lambda light chain or any of the five heavy chains.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Purification notes
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The kappa light chain alternatively known as Ig kappa chain is a component of immunoglobulins which are important for immune response. This protein has a molecular mass of roughly 25 kDa. It predominantly expresses in B lymphocytes where it pairs with heavy chains to form antibodies. Its expression is indicative of mature B cell functions serving as a marker for certain types of immune cells. The kappa light chain can also be detected outside of cells circulating in the blood and other bodily fluids.
Biological function summary

Kappa light chains are integral to the structure and function of antibodies. As part of the immunoglobulin molecule these chains contribute to antigen specificity by combining with heavy chains. Together they form the antigen-binding site. The kappa light chain is not part of a multiprotein complex; rather it directly participates in the antibody response. The presence of either kappa or lambda light chains can determine the particularities of antibody characteristics.

Pathways

Kappa light chains are elements of the immunological pathways notably the adaptive immune response. They interact with other proteins like immunoglobulin heavy chains to neutralize pathogens. The constant region of the kappa chain plays a role in determining the isotype of immunoglobulins which affects how antibodies mediate immune effector functions. Cross-linking of surface immunoglobulin by antigens can trigger B cell activation an essential step in the adaptive immune system.

Kappa light chains associate closely with multiple myeloma and certain types of lymphomas. Overproduction of kappa light chains in these diseases results in high levels detectable in the serum or urine which can be used diagnostically as markers. Also dysregulation of kappa chains correlates with autoimmune disorders whereby the immune system incorrectly targets its tissues. In disorders like these the interplay between kappa and lambda chains often arises showing imbalance between the two as a sign of abnormal B cell activity.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed : 20176268, PubMed : 22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed : 17576170, PubMed : 20176268).
See full target information IGKC

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Oncology reports 44:1355-1364 PubMed32945483

2020

SUMOylation of HSP27 regulates PKM2 to promote esophageal squamous cell carcinoma progression.

Applications

Unspecified application

Species

Unspecified reactive species

Xiao Zhang,Tao Liu,Shutao Zheng,Qing Liu,Tongxue Shen,Xiujuan Han,Qiqi Zhang,Lifei Yang,Xiaomei Lu
View all publications

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