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AB20098

Anti-Lambda Light chain antibody

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(1 Publication)

Goat Polyclonal LV151 antibody. Suitable for ELISA and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Native Full Length Protein corresponding to Human IGLV1-51.

View Alternative Names

Immunoglobulin lambda variable 1-51, Ig lambda chain V-I region BL2, Ig lambda chain V-I region EPS, Ig lambda chain V-I region NEW, Ig lambda chain V-I region NIG-64, IGLV1-51

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ELISA

applications

Immunogen

Native Full Length Protein corresponding to Human IGLV1-51.

P01701

Specificity

Monospecific by immunoelectrophoresis when tested against pooled human plasma and twice concentrated pooled human serum.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Delipidation and ion exchange chromatography. Product is 0.2um filtered.
Storage buffer
Preservative: 0.1% Sodium azide Constituents: Tris buffered saline
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
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

Lambda Light Chain also known as lambda chain or lambda protein forms a part of immunoglobulins (antibodies). Its mass typically ranges between 22 to 24 kDa. This protein is expressed primarily in B cells. Specifically it pairs with heavy chains to form the complete antibody molecule. It participates in the antigen recognition process supporting the immune system's defense mechanisms.
Biological function summary

Lambda Light Chain participates in immunological functions by contributing to the antigen-binding site of antibodies. It exists as a part of the immunoglobulin complex. The lambda chain alongside heavy chains forms the variable part of antibodies allowing specificity in antigen recognition. Its variation leads to a diverse antibody repertoire which is important for recognizing a wide range of pathogens.

Pathways

Lambda Light Chain fits into pathways involving adaptive immune responses. It is important in antigen processing and presentation pathways. In this context it interacts with the heavy chains which together drive the specificity and efficiency of immune response pathways. It also associates with proteins like the major histocompatibility complex (MHC) which facilitates antigen presentation to T cells.

Lambda Light Chain associates with multiple myeloma a cancer of plasma cells and light chain amyloidosis a disorder where light chains accumulate as amyloid fibrils in tissues. In these conditions proteins like immunoglobulin heavy chain and albumin often interact with or are affected by lambda chains providing insights into disease mechanisms and potential targets for therapeutic intervention.

Product protocols

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

Target data

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed : 24600447). 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 IGLV1-51

Publications (1)

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

Frontiers in microbiology 9:1559 PubMed30061873

2018

Bacterial Outer Membrane Vesicles Induce Vitronectin Release Into the Bronchoalveolar Space Conferring Protection From Complement-Mediated Killing.

Applications

Unspecified application

Species

Unspecified reactive species

Magnus Paulsson,Karlhans F Che,Jonas Ahl,Johan Tham,Linda Sandblad,Margaretha E Smith,Ingemar Qvarfordt,Yu-Ching Su,Anders Lindén,Kristian Riesbeck
View all publications

Product promise

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