Recombinant Human Dynein Light Chain 1, Cytoplasmic Domain (DYNLL1) Protein (GST)

Name: Recombinant Human Dynein Light Chain 1, Cytoplasmic Domain (DYNLL1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04500P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Dynein Light Chain 1, Cytoplasmic Domain (DYNLL1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P63167
Target Symbol	DYNLL1
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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Expression Range	1-89aa
Protein Length	Full Length
Mol. Weight	37.4kDa
Research Area	Apoptosis
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

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.
Subcellular Location	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.
Protein Families	Dynein light chain family
Database References	HGNC: 15476 OMIM: 601562 KEGG: hsa:8655 STRING: 9606.ENSP00000242577 UniGene: PMID: 30018294 High PIN expression is associated with Dilated Hearts. PMID: 27481317 An expanded list of LC8 binding partners revealed the evolutionary plasticity of binding partners despite the highly conserved binding interface. In addition, it also highlighted a novel, conserved function of LC8 in the upstream regulation of the Hippo signaling pathway. PMID: 29240760 DLC1 binding to nNOS-calmodulin complex does not affect the electron transport from the reductase to the oxygenase domain. PMID: 26923072 NMR-derived secondary chemical shifts and relaxation properties show that the Chica LC8 binding domain is essentially disordered with a dynamically restricted segment in one linker between motifs. PMID: 26652654 Studies indicate that dynein light chain LC8 has been termed an intrinsically disordered proteins (IDPs) dimerization 'hub' protein. PMID: 26226419 DLC1 binding motif in L is involved in cytoskeleton localization and reorganization, primary transcription regulation by DLC1, and regulation of cellular DLC1 gene expression. PMID: 26157129 The dynein light intermediate chain has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins. PMID: 25272277 Authors demonstrate that the interaction between ebola virus VP35 and dynein LC8 is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis. PMID: 25741013 Overall, this study demonstrates the novel interaction between HIV-1 integrase and cellular DYNLL1 proteins and suggests the requirement of this virus-cell interaction for proper uncoating and efficient reverse transcription of HIV-1. PMID: 25568209 Structural analysis of LC8 with both Nek9 peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 to LC8 upon phosphorylation on Ser(944) within the Nek9 sequence PMID: 23482567 Dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis. PMID: 23589491 Overexpressed human LC8 inhibits mouse osteoclast differentiation by regulating NF-kappaB & MAPK pathways and suppressing RANKL signaling. PMID: 23293355 DYNLL1 interacted with a spindle-microtubule-associated adaptor formed by CHICA and HMMR via TQT motifs in CHICA. PMID: 22965910 appropriate levels of ternary complex components are critical for dynein-dependent spindle positioning in HeLa cells and C. elegans embryos PMID: 23027904 Cytosolic mfGbeta is recruited to dynein by Nudel and transported to the centrosome for rapid sequestration and degradation. PMID: 22430153 Study found the secretion of calu-1/2-EGFP required microtubule integrity, and that calu-1/2-EGFP-containing vesicles were transported by the motor proteins Kif5b and cytoplasmic dynein. PMID: 22514732 The ASCIZ-DYNLL1 feedback loop represents a novel mechanism for auto-regulation of gene expression, where the gene product directly inhibits the transcriptional activator while bound at its own promoter. PMID: 22167198 The study uses thermodynamics and dynamics measurements of LC8 complexes to group LC8 binding partners in two categories: those whose binding is enthalpically driven and those that are entropically favored. PMID: 21621319 these results imply a potential cellular interference between DYNLL1 and ATMIN functions. PMID: 21971545 results significantly widen the scope of the human interactome around DYNLL and will certainly shed more light on the biological functions and organizing role of DYNLL in the human and other eukaryotic interactomes PMID: 21533121 DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9. PMID: 21454704 Data demonstrate the direct interaction between DYNLL1 and peptides derived from ASFV p54 and gephyrin interacting sequences. PMID: 21094642 effect of glycosylation on protein folding thermodynamics and kinetics PMID: 20936810 Data suggest that MTOC-directed movement of lytic granules in NK cells is independent of actin and microtubule reorganization, dependent on dynein motor function, occurs before MTOC polarization, and does not require a commitment to cytotoxicity. PMID: 20444980 the thermodynamic and kinetic fine-tuning of binding of various ligands to DYNLL could have physiological relevance in its interaction network. PMID: 20889982 Data provide the first trafficking regulatory role for Crmp2 in non-neuronal cells and support a model in which Crmp2 is an important endocytic regulatory protein that links MICAL-L1.EHD1-based vesicular transport to dynein motors. PMID: 20801876 Data identify GRINL1A as a membrane-associated DYNLL1 binding partner and suggest that additional DYNLL1-binding partners are present near this glutamate channel homolog. PMID: 20412299 the regulation of DLC1 by p21-activated kinase 1 is a novel mechanism by which a signaling kinase might influence macropinocytosis PMID: 15504720 LC8 binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation PMID: 15611139 PAX6 interacts with HOMER3, DNCL1, and TRIM11. Three C-terminal PAX6 mutations, previously identified in patients with eye malformations, all reduced or abolished the interactions. PMID: 16098226 the DLC1-KIBRA interaction is essential for ER transactivation in breast cancer cells PMID: 16684779 PIN not only inhibits nitric oxide but also .O(2)(-) production from nitric oxide synthase 1 PMID: 16781079 dynein light chain 1 represents a novel anchoring protein for RasGRP3 that may regulate subcellular localization of the exchange factor PMID: 17012239 we established for the first time expression of PIN/LC8 in human mast cells PMID: 17169380 findings reveal a previously unrecognized regulatory mechanism of DLC1 in which the Ser(88) phosphorylation acts as a molecular switch for the transition of DLC1 from dimer to monomer PMID: 18084006 LC8 binds IkappaBalpha in a redox-dependent manner and thereby prevents its phosphorylation by IKK. TRP14 contributes to this inhibitory activity by maintaining LC8 in a reduced state. PMID: 18579519 pH dependent unfolding characteristics of DLC8 dimer: Residue level details from NMR. PMID: 18692162 The data indicated the presence of intermediates along the equilibrium unfolding transition; the hydrogen exchange data suggested that the DLC8 molecule has differential stability in its various segments. PMID: 18767155 Hierarchy in guanidine unfolding of DYNLL1 dimer is reported. PMID: 19032974 LC8 facilitates nuclear import of Pak1 and this function is indispensable during vertebrate development PMID: 19557173

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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