TBCC / Unconjugated /
Product Details
Description | Microtubules, the primary component of the cytoskeletal network, are highly dynamic structures composed of α/β Tubulin heterodimers. Biosynthesis of functional microtubules involve the participation of several chaperones, termed tubulin folding cofactors A (TBCA), D (TBCD), E (TBCE) and C (TBCC), that act on folding intermediates downstream of the cytosolic chaperonin, alternatively named TCP. TBCC (Tubulin-specific chaperone C), also known as β Tubulin-folding cofactor C or CFC, is a 346 amino acid protein belonging to the TBCD family. Interaction with TBCC causes the release of tubulin polypeptides that are committed to the native state. TBCC shares significant homology with X-linked retinitis pigmentosa 2 gene RP2, in which mutations cause the progressive degeneration of photoreceptor cells. | |
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Conjugate | Unconjugated | |
Clone | ||
Target Species | Human | |
Applications | ICC, WB, IHC | |
Supplier | HuaBio | |
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About TBCC
Cofactor C is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. [provided by RefSeq, Jul 2008]
Cofactor C is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. [provided by RefSeq, Jul 2008]
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