Lambda Light Chain Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC-P, IHC-F, IF, E |
---|---|
Primary Accession | P01701 |
Reactivity | Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 22.5 KDa |
Physical State | Liquid |
Immunogen | KLH conjugated synthetic peptide derived from human Lambda Light Chain |
Epitope Specificity | 41-106/106 |
Isotype | IgG |
Purity | affinity purified by Protein A |
Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
SUBCELLULAR LOCATION | Cytoplasmic |
SIMILARITY | Contains 1 Ig-like (immunoglobulin-like) domain. |
Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
Background Descriptions | All five immunoglobulin classes share the same basic four polypeptide chain structure of two heavy-chains and two light chains. There are five heavy chain types, and two light-chain types (Kappa and Lambda) both having a molecular weight of 22.5kDa. Any heavy-chain type can associate with either light-chain type, but on any immunoglobulin molecule both light-chains are of the same type. Kappa and Lambda consist of a variable region and a constant region and can easily be differentiated by the antigenic properties of the constant region. |
Other Names | Immunoglobulin lambda variable 1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7}, 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 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7} |
---|---|
Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ELISA=1:5000-10000 |
Format | 0.01M TBS(pH7.4), 0.09% (W/V) sodium azide and 50% Glyce |
Storage | Store at -20 ℃ for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 ℃. |
Name | IGLV1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7} |
---|---|
Function | 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). |
Cellular Location | Secreted. Cell membrane |

Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.

If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.