Concanavalin A: Difference between revisions
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== Concanavalin A == | |||
[[File:3CNA_Concanavalin_A.png|thumb|right|300px|Structure of Concanavalin A]] | |||
'''Concanavalin A''' (Con A) is a [[lectin]] protein derived from the [[jack bean]] plant, ''Canavalia ensiformis''. It is widely used in [[biochemistry]] and [[cell biology]] for its ability to bind specifically to certain [[carbohydrates]]. | |||
== Structure == | |||
Concanavalin A is a [[homotetramer]], meaning it is composed of four identical subunits. Each subunit has a molecular weight of approximately 26,000 [[daltons]]. The protein binds to [[mannose]] and [[glucose]] residues, which are common components of [[glycoproteins]] and [[glycolipids]]. | |||
== Function == | |||
Con A is known for its ability to agglutinate [[cells]] and [[precipitate]] [[glycoconjugates]]. This property is utilized in various laboratory techniques, such as [[affinity chromatography]], to purify glycoproteins. Con A can also be used to study cell surface [[glycans]] and to stimulate [[lymphocytes]] in [[immunological]] research. | |||
== Applications == | |||
=== Biochemical Research === | |||
In [[biochemical research]], Concanavalin A is used to isolate and study glycoproteins. Its ability to bind specifically to mannose and glucose residues makes it a valuable tool for identifying and characterizing [[glycosylation]] patterns on proteins. | |||
=== Cell Biology === | |||
In [[cell biology]], Con A is used to study cell surface carbohydrates. It can be used to label cells for [[fluorescence microscopy]] or to sort cells using [[flow cytometry]]. Con A is also used to stimulate [[T cells]] in [[immunology]] experiments, as it can mimic the effects of [[antigen]]s. | |||
=== Medical Research === | |||
Con A has been used in [[medical research]] to study [[cancer]] and [[autoimmune diseases]]. Its ability to bind to specific carbohydrates on cell surfaces can help in the identification of [[tumor markers]] and in the study of [[cell signaling]] pathways. | |||
== Related pages == | |||
* [[Lectin]] | |||
* [[Glycoprotein]] | |||
* [[Affinity chromatography]] | |||
* [[Cell surface receptor]] | |||
[[Category:Proteins]] | [[Category:Proteins]] | ||
[[Category: | [[Category:Biochemistry]] | ||
[[Category:Cell biology]] | |||
Latest revision as of 11:09, 15 February 2025
[edit]

Concanavalin A (Con A) is a lectin protein derived from the jack bean plant, Canavalia ensiformis. It is widely used in biochemistry and cell biology for its ability to bind specifically to certain carbohydrates.
Structure[edit]
Concanavalin A is a homotetramer, meaning it is composed of four identical subunits. Each subunit has a molecular weight of approximately 26,000 daltons. The protein binds to mannose and glucose residues, which are common components of glycoproteins and glycolipids.
Function[edit]
Con A is known for its ability to agglutinate cells and precipitate glycoconjugates. This property is utilized in various laboratory techniques, such as affinity chromatography, to purify glycoproteins. Con A can also be used to study cell surface glycans and to stimulate lymphocytes in immunological research.
Applications[edit]
Biochemical Research[edit]
In biochemical research, Concanavalin A is used to isolate and study glycoproteins. Its ability to bind specifically to mannose and glucose residues makes it a valuable tool for identifying and characterizing glycosylation patterns on proteins.
Cell Biology[edit]
In cell biology, Con A is used to study cell surface carbohydrates. It can be used to label cells for fluorescence microscopy or to sort cells using flow cytometry. Con A is also used to stimulate T cells in immunology experiments, as it can mimic the effects of antigens.
Medical Research[edit]
Con A has been used in medical research to study cancer and autoimmune diseases. Its ability to bind to specific carbohydrates on cell surfaces can help in the identification of tumor markers and in the study of cell signaling pathways.