DYNLT1 Human
Dynein light chain Tctex-type 1, Protein CW-1, T-complex testis-specific protein 1 homolog, DYNLT1, TCTEL1, TCTEX-1, TCTEX1, CW-1.
Description
DYNLT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-113 a.a.) and having a molecular mass of 14.6kDa.
DYNLT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Dynein light chain Tctex-type 1 (DYNLT1), a member of the dynein light chain Tctex-type family, is a dynein light chain involved in cargo binding. As one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex, DYNLT1 is believed to play a role in linking dynein to cargos and adapter proteins that regulate dynein function. Cytoplasmic dynein, a crucial motor protein complex, is responsible for minus-end, microtubule-based motile processes. Each dynein complex comprises two heavy chains with ATPase and motor activities, along with a group of accessory polypeptides.
Recombinant Human DYNLT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 133 amino acids (1-113 a.a.). With a molecular weight of 14.6 kDa, DYNLT1 is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
The DYNLT1 protein solution (1 mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 30% glycerol, and 0.1 M NaCl.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal long-term stability, adding a carrier protein (0.1% HSA or BSA) is advisable. Avoid repeated freeze-thaw cycles.
Dynein light chain Tctex-type 1, Protein CW-1, T-complex testis-specific protein 1 homolog, DYNLT1, TCTEL1, TCTEX-1, TCTEX1, CW-1.
MGSSHHHHHH SSGLVPRGSH MEDYQAAEET AFVVDEVSNI VKEAIESAIG GNAYQHSKVN QWTTNVVEQT LSQLTKLGKP FKYIVTCVIM QKNGAGLHTA SSCFWDSSTD GSCTVRWENK TMYCIVSAFG LSI.
Product Science Overview
The cytoplasmic dynein motor complex consists of two heavy chains that have ATPase and motor activities, along with several accessory polypeptides, including the light chain Tctex-type 1 . The primary role of DYNLT1 is to act as a non-catalytic accessory component of the dynein complex, linking dynein to various cargos and adapter proteins that regulate its function .
DYNLT1 is involved in the intracellular retrograde motility of vesicles and organelles along microtubules. It binds to transport cargos and plays a crucial role in apical cargo transport, such as rhodopsin-bearing vesicles in polarized epithelia . Additionally, it may serve as an accessory component of axonemal dynein .
DYNLT1 has several dynein-independent functions, including roles in G protein signaling activation and neuronal growth . It is selectively enriched in proliferating neural progenitors of both embryonic and adult brains . This protein also interacts with viral proteins, such as the minor capsid protein L2 of human papillomavirus, and is required for dynein-mediated delivery of viral nucleic acid to the host nucleus .
Moreover, DYNLT1 interacts with oncogenic nucleoporins to disrupt gene regulation and cause leukemic transformation . It plays a role in neuronal morphogenesis, independent of cytoplasmic dynein, by enhancing Rac1 activity and regulating the actin cytoskeleton .
Recombinant human DYNLT1 is used in research to study its function and interactions within the cell. It is also utilized in assays to investigate its role in disease mechanisms and to develop potential therapeutic strategies.
