Rabbit anti-Human Lambda Light chain Polyclonal Antibody | anti-IGLV1-51 antibody

Lambda Light chain Antibody

Cat. Num. AAA9629357

• Reactivity: Human
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Synonyms: Lambda Light chain; Polyclonal Antibody; Lambda Light chain Antibody; anti-IGLV1-51 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Lambda Light chain Antibody detects endogenous levels of total Lambda Light chain.
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-IGLV1-51 antibody: ELISA (EIA)(peptide)
• Application Notes: ELISA(peptide): 1:20000-1:40000
• Immunogen: A synthesized peptide derived from Human MYOCD.
• Conjugation: Unconjugated
• Subunit Structure: Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.
• Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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. 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.
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Product Categories/Family for anti-IGLV1-51 antibody

Secreted; Cell membrane; Primary

NCBI and Uniprot Product Information

• NCBI GI #: 126541
• NCBI GeneID: 3535
• UniProt Accession #: P01701; P01842
• Molecular Weight: ~22.5kDa
• NCBI Official Full Name: Ig lambda chain V-I region NEW
• UniProt Protein Name: Ig lambda chain V-I region NEW
• Protein Family: Immunoglobulin lambda variable
• UniProt Entry Name: LV103_HUMAN

Uniprot Description

IGLV1-51: V segment of the variable region of immunoglobulins light chain that participates to the antigen recognition. Immunoglobulins (Igs), also known as antibodies, are membrane- bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors which, upon binding of a specific antigen (Ag), trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs 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 region of one heavy chain, together with that of its associated light chain. Thus, each Ig has two antigen binding sites with remarkable affinity for a particular antigen. The variable regions are assembled by a process called V(D)J recombination and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation for a particular Ag (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds. {ECO:0000303|PubMed:20176268}