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The recombinant Human DYNLL1 protein synthesis in e.coli cells necessitates the incorporation of a DNA fragment encoding the Human DYNLL1 protein (1-89aa) into a plasmid vector, followed by the transformation of this vector into e.coli cells. After screening for positive cells, they are cultured and induced to express the DYNLL1 protein. The protein carries a N-terminal GST tag. Cell lysis is performed to gather the recombinant Human DYNLL1 protein, which undergoes affinity purification and is then analyzed using SDS-PAGE and subsequent staining of the gel with Coomassie Brilliant Blue. The purity of the resulting recombinant Human DYNLL1 protein reaches up to 90%.
The recombinant Human DYNLL1 protein synthesis in e.coli cells necessitates the incorporation of a DNA fragment encoding the Human DYNLL1 protein (1-89aa) into a plasmid vector, followed by the transformation of this vector into e.coli cells. After screening for positive cells, they are cultured and induced to express the DYNLL1 protein. The protein carries a N-terminal GST tag. Cell lysis is performed to gather the recombinant Human DYNLL1 protein, which undergoes affinity purification and is then analyzed using SDS-PAGE and subsequent staining of the gel with Coomassie Brilliant Blue. The purity of the resulting recombinant Human DYNLL1 protein reaches up to 90%.
| Cat.No | ACP04521 | Target Name | DYNLL1 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 1-89aa | Mol Weight | 37.4kDa |
| Protein Length | Full length | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P63167 |
|---|
Uniprot Id
P63167
Target Species
Human
Target Name
DYNLL1
Target Full Name
Dynein light chain 1, cytoplasmic
Target Function
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.; Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.; Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.; Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.
Target Subcellular Location
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.
Target Protein Families
Dynein light chain family
Target Tissue Specificity
Ubiquitous. Expressed in testis.
Target Research Area
Apoptosis
Target Synonyms
8 kDa dynein light chain; 8kDLC; Cytoplasmic dynein light polypeptide ; DLC1; DLC8; DNCL1; DNCLC1; DYL1_HUMAN; Dynein ; cytoplasmic; light chain 1; Dynein light chain 1 cytoplasmic; Dynein light chain 1; cytoplasmic; Dynein light chain LC8 type 1; Dynein light chain LC8-type 1; Dynein; cytoplasmic; light polypeptide 1; Dynein; light chain; LC8-type 1; DYNLL1; HDLC1; LC8; LC8a; MGC126137; MGC126138; MGC72986; PIN; Protein inhibitor of neuronal nitric oxide synthase; Protein inhibitor of neuronal NOS
Target Background
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1, 200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.
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