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Immunoglobulin kappa variable

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V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition .

Below are the list of possible Immunoglobulin kappa variable products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Immunoglobulin kappa variable 1-12

 Immunoglobulin kappa variable 1-12 ELISA Kit
 Immunoglobulin kappa variable 1-12 Recombinant
 Immunoglobulin kappa variable 1-12 Antibody
IGKV1-12: 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 expa
>>>
nsion 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: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}
 IGKV1-12 ELISA Kit
 IGKV1-12 Recombinant
 IGKV1-12 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1-16

 Immunoglobulin kappa variable 1-16 ELISA Kit
 Immunoglobulin kappa variable 1-16 Recombinant
 Immunoglobulin kappa variable 1-16 Antibody
Also known as Immunoglobulin kappa variable 1-16 (Ig kappa chain V-I region BAN).
IGKV1-16: 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 (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: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}
 IGKV1-16 ELISA Kit
 IGKV1-16 Recombinant
 IGKV1-16 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1-17

 Immunoglobulin kappa variable 1-17 ELISA Kit
 Immunoglobulin kappa variable 1-17 Recombinant
 Immunoglobulin kappa variable 1-17 Antibody
Also known as Immunoglobulin kappa variable 1-17 (Ig kappa chain V-I region Gal) (Ig kappa chain V-I region WEA).
IGKV1-17: V segment of the variable domain of immunoglobulins light chain that participates to 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, th
>>>
e 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: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}
 IGKV1-17 ELISA Kit
 IGKV1-17 Recombinant
 IGKV1-17 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1-33

 Immunoglobulin kappa variable 1-33 ELISA Kit
 Immunoglobulin kappa variable 1-33 Recombinant
 Immunoglobulin kappa variable 1-33 Antibody
Also known as Immunoglobulin kappa variable 1-33 (Ig kappa chain V-I region AU) (Ig kappa chain V-I region Ka).
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-bo
>>>
und 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:20176268, PubMed:17576170).
 IGKV1-33 ELISA Kit
 IGKV1-33 Recombinant
 IGKV1-33 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1-39

 Immunoglobulin kappa variable 1-39 ELISA Kit
 Immunoglobulin kappa variable 1-39 Recombinant
 Immunoglobulin kappa variable 1-39 Antibody
Also known as Immunoglobulin kappa variable 1-39 (Ig kappa chain V-I region DEE) (Ig kappa chain V-I region Hau) (Ig kappa chain V-I region Mev) (Ig kappa chain V-I region OU) (Ig kappa chain V-I region Walker).
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 gl
>>>
ycoproteins 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:20176268, PubMed:17576170).
 IGKV1-39 ELISA Kit
 IGKV1-39 Recombinant
 IGKV1-39 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1-5

 Immunoglobulin kappa variable 1-5 ELISA Kit
 Immunoglobulin kappa variable 1-5 Recombinant
 Immunoglobulin kappa variable 1-5 Antibody
Also known as Immunoglobulin kappa variable 1-5 (Ig kappa chain V-I region CAR) (Ig kappa chain V-I region EU) (Ig kappa chain V-I region HK102) (Ig kappa chain V-I region Kue).
IGKV1-5: 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 produ
>>>
ced 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}

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: extracellular region; plasma membrane

Molecular Function: serine-type endopeptidase activity

Biological Process: complement activation; complement activation, classical pathway; immune response; immunoglobulin production; receptor-mediated endocytosis; regulation of immune response
 IGKV1-5 ELISA Kit
 IGKV1-5 Recombinant
 IGKV1-5 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1D-12

 Immunoglobulin kappa variable 1D-12 ELISA Kit
 Immunoglobulin kappa variable 1D-12 Recombinant
 Immunoglobulin kappa variable 1D-12 Antibody
Also known as Immunoglobulin kappa variable 1D-12 (Ig kappa chain V-I region Wes).
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 (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:20176268, PubMed:17576170).
 IGKV1D-12 ELISA Kit
 IGKV1D-12 Recombinant
 IGKV1D-12 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1D-16

 Immunoglobulin kappa variable 1D-16 ELISA Kit
 Immunoglobulin kappa variable 1D-16 Recombinant
 Immunoglobulin kappa variable 1D-16 Antibody
Also known as Immunoglobulin kappa variable 1D-16 (Ig kappa chain V-I region HK146) (Ig kappa chain V-I region HK189).
KV109: V region of the variable domain of immunoglobulin light chains that participates in 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 m
>>>
embrane-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: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}

Protein type: Immunoglobulin superfamily

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: external side of plasma membrane; extracellular region; extracellular space; plasma membrane

Molecular Function: antigen binding; serine-type endopeptidase activity

Biological Process: B cell receptor signaling pathway; complement activation; complement activation, classical pathway; defense response to bacterium; innate immune response; phagocytosis, engulfment; phagocytosis, recognition; positive regulation of B cell activation; receptor-mediated endocytosis; regulation of immune response; retinal homeostasis

Disease: Immunoglobulin Kappa Light Chain Deficiency
 IGKV1D-16 ELISA Kit
 IGKV1D-16 Recombinant
 IGKV1D-16 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1D-33

 Immunoglobulin kappa variable 1D-33 ELISA Kit
 Immunoglobulin kappa variable 1D-33 Recombinant
 Immunoglobulin kappa variable 1D-33 Antibody
Also known as Immunoglobulin kappa variable 1D-33 (Ig kappa chain V-I region AG) (Ig kappa chain V-I region Bi) (Ig kappa chain V-I region Lay) (Ig kappa chain V-I region Ni) (Ig kappa chain V-I region Rei) (Ig kappa chain V-I region Roy) (Ig kappa chain V-I region Scw) (Ig kappa chain V-I region WAT).
V region of the variable domain of immunoglobulin light chains that participates in the antig
>>>
en 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 (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:20176268, PubMed:17576170).
 IGKV1D-33 ELISA Kit
 IGKV1D-33 Recombinant
 IGKV1D-33 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 1D-39

 Immunoglobulin kappa variable 1D-39 ELISA Kit
 Immunoglobulin kappa variable 1D-39 Recombinant
 Immunoglobulin kappa variable 1D-39 Antibody
Also known as Immunoglobulin kappa variable 1D-39 (Ig kappa chain V-I region Daudi).
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 a
>>>
s 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:20176268, PubMed:17576170).
 IGKV1D-39 ELISA Kit
 IGKV1D-39 Recombinant
 IGKV1D-39 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 2-28

 Immunoglobulin kappa variable 2-28 ELISA Kit
 Immunoglobulin kappa variable 2-28 Recombinant
 Immunoglobulin kappa variable 2-28 Antibody
IGKV2-28: 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 expa
>>>
nsion 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: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}
 IGKV2-28 ELISA Kit
 IGKV2-28 Recombinant
 IGKV2-28 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 2-30

 Immunoglobulin kappa variable 2-30 ELISA Kit
 Immunoglobulin kappa variable 2-30 Recombinant
 Immunoglobulin kappa variable 2-30 Antibody
Also known as Immunoglobulin kappa variable 2-30 (Ig kappa chain V-II region RPMI 6410).
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 ser
>>>
ve 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:20176268, PubMed:17576170).
 IGKV2-30 ELISA Kit
 IGKV2-30 Recombinant
 IGKV2-30 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 2D-28

 Immunoglobulin kappa variable 2D-28 ELISA Kit
 Immunoglobulin kappa variable 2D-28 Recombinant
 Immunoglobulin kappa variable 2D-28 Antibody
Also known as Immunoglobulin kappa variable 2D-28 (Ig kappa chain V-II region FR) (Ig kappa chain V-II region GM607) (Ig kappa chain V-II region MIL) (Ig kappa chain V-II region TEW).
IGKV2D-28: 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 produ
>>>
ced 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.

Chromosomal Location of Human Ortholog: 22q11.1
 IGKV2D-28 ELISA Kit
 IGKV2D-28 Recombinant
 IGKV2D-28 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 2D-30

 Immunoglobulin kappa variable 2D-30 ELISA Kit
 Immunoglobulin kappa variable 2D-30 Recombinant
 Immunoglobulin kappa variable 2D-30 Antibody
IGKV2D-30: 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 exp
>>>
ansion 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: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}
 IGKV2D-30 ELISA Kit
 IGKV2D-30 Recombinant
 IGKV2D-30 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 2D-40

 Immunoglobulin kappa variable 2D-40 ELISA Kit
 Immunoglobulin kappa variable 2D-40 Recombinant
 Immunoglobulin kappa variable 2D-40 Antibody
Also known as Immunoglobulin kappa variable 2D-40 (Ig kappa chain V-II region Cum).
IGKV2-40: 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 immunoglobulin
>>>
s 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: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}

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: extracellular region; plasma membrane

Molecular Function: serine-type endopeptidase activity

Biological Process: complement activation; complement activation, classical pathway; receptor-mediated endocytosis; regulation of immune response
 IGKV2D-40 ELISA Kit
 IGKV2D-40 Recombinant
 IGKV2D-40 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 3-11

 Immunoglobulin kappa variable 3-11 ELISA Kit
 Immunoglobulin kappa variable 3-11 Recombinant
 Immunoglobulin kappa variable 3-11 Antibody
Also known as Immunoglobulin kappa variable 3-11 (Ig kappa chain V-III region VG).
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 (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:20176268, PubMed:17576170).
 IGKV3-11 ELISA Kit
 IGKV3-11 Recombinant
 IGKV3-11 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 3-15

 Immunoglobulin kappa variable 3-15 ELISA Kit
 Immunoglobulin kappa variable 3-15 Recombinant
 Immunoglobulin kappa variable 3-15 Antibody
Also known as Immunoglobulin kappa variable 3-15 (Ig kappa chain V-III region CLL) (Ig kappa chain V-III region POM).
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 membr
>>>
ane-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:20176268, PubMed:17576170).
 IGKV3-15 ELISA Kit
 IGKV3-15 Recombinant
 IGKV3-15 Antibody
Table BarTOPTable Bar
 

Immunoglobulin kappa variable 3-20

 Immunoglobulin kappa variable 3-20 ELISA Kit
 Immunoglobulin kappa variable 3-20 Recombinant
 Immunoglobulin kappa variable 3-20 Antibody
IGKV3D-20: 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 exp
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ansion 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: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}
 IGKV3D-20 ELISA Kit
 IGKV3D-20 Recombinant
 IGKV3D-20 Antibody
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Immunoglobulin kappa variable 4-1

 Immunoglobulin kappa variable 4-1 ELISA Kit
 Immunoglobulin kappa variable 4-1 Recombinant
 Immunoglobulin kappa variable 4-1 Antibody
Also known as Immunoglobulin kappa variable 4-1 (Ig kappa chain V-IV region B17) (Ig kappa chain V-IV region JI) (Ig kappa chain V-IV region Len) (Ig kappa chain V-IV region STH).
IGKV4-1: 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 pro
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duced 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:22158414, PubMed:20176268). 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}

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: extracellular region; plasma membrane

Molecular Function: serine-type endopeptidase activity

Biological Process: complement activation; complement activation, classical pathway; immune response; immunoglobulin production; receptor-mediated endocytosis; regulation of immune response
 IGKV4-1 ELISA Kit
 IGKV4-1 Recombinant
 IGKV4-1 Antibody
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Immunoglobulin kappa variable 5-2

 Immunoglobulin kappa variable 5-2 ELISA Kit
 Immunoglobulin kappa variable 5-2 Recombinant
 Immunoglobulin kappa variable 5-2 Antibody
Also known as Immunoglobulin kappa variable 5-2 (Ig kappa chain V region EV15).
IGKV5-2: 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 ser
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ve 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: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}

Protein type: Unknown function

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: extracellular region; plasma membrane

Molecular Function: serine-type endopeptidase activity

Biological Process: complement activation; complement activation, classical pathway; receptor-mediated endocytosis; regulation of immune response
 IGKV5-2 ELISA Kit
 IGKV5-2 Recombinant
 IGKV5-2 Antibody
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