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抗人 TEKT2 抗体对
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抗人 TEKT2 抗体对

01AB02774

Tektin 2 (TEKT2) is a cytoskeletal protein characterized by a long coiled-coil domain that enables it to form dimers and interact with other tektin proteins, contributing to the structural integrity of cilia and flagella, particularly as a component of outer doublet microtubules. TEKT2 is essential for the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia, thereby playing a crucial role in the stability and function of these motile structures. The protein’s structure includes conserved alpha-helical segments and a tektin-specific nonapeptide sequence, which is believed to be important for binding to tubulin and maintaining the periodicity required for microtubule organization. Mutations or dysfunction in TEKT2 have been associated with defects in sperm motility and male infertility, as impaired flagellar structure can lead to asthenozoospermia, highlighting its clinical relevance in reproductive health.

Human
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技术参数

靶点基因名
TEKT2
蛋白别名
tektin 2; TEKT2
UniProt
Q9UIF3
物种
Human

产品详情

靶点名称
TEKT2
蛋白名称
tektin 2
蛋白别名
Tektin-2; Tektin-t; Testicular tektin; Testicular tektin B1-like protein; TEKTB1; Tektin-B1
靶点基因名
TEKT2
UniProt
Q9UIF3
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Tektin 2 (TEKT2) is a cytoskeletal protein characterized by a long coiled-coil domain that enables it to form dimers and interact with other tektin proteins, contributing to the structural integrity of cilia and flagella, particularly as a component of outer doublet microtubules. TEKT2 is essential for the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia, thereby playing a crucial role in the stability and function of these motile structures. The protein’s structure includes conserved alpha-helical segments and a tektin-specific nonapeptide sequence, which is believed to be important for binding to tubulin and maintaining the periodicity required for microtubule organization. Mutations or dysfunction in TEKT2 have been associated with defects in sperm motility and male infertility, as impaired flagellar structure can lead to asthenozoospermia, highlighting its clinical relevance in reproductive health.