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AB20098

Anti-Lambda Light chain 抗体

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.

別名を表示する

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

宿主種

Goat

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Human

アプリケーション

ELISA

applications

免疫原

Native Full Length Protein corresponding to Human IGLV1-51.

P01701

特異性

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

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ELISA" : {"fullname" : "ELISA", "shortname":"ELISA"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ELISA-species-checked": "guaranteed", "ELISA-species-dilution-info": "", "ELISA-species-notes": "<p></p>" } } }

出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Protein G
精製に関する特記事項
Delipidation and ion exchange chromatography. Product is 0.2um filtered.
バッファー組成
Preservative: 0.1% Sodium azide Constituents: Tris buffered saline
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
保管に関する情報
Avoid freeze / thaw cycle

補足情報

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.

製品プロトコール

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ターゲットの情報

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

文献 (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

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