Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

DYNLL1

Uniprot No.

P63167

Research Area

Apoptosis

Alternative Names

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)

Source

E.coli

Expression Region

1-89aa

Target Protein Sequence

MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

37.4kDa

Protein Length

Full Length

Tag Info

N-terminal GST-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

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%.

Target Background

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.

Gene References into Functions

It has been found that APC2 localizes as distinct clusters along microtubule bundles in dendrites, and that this localization is driven by LC8-binding and two separate microtubule-interacting domains. 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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Subcellular Location

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.

Protein Families

Dynein light chain family

Tissue Specificity

Ubiquitous. Expressed in testis.

Database Links

HGNC: 15476

OMIM: 601562

KEGG: hsa:8655

STRING: 9606.ENSP00000242577

UniGene: Hs.5120

Code	CSB-RP012844h
Abbreviation	Recombinant Human DYNLL1 protein
MSDS	MSDS Datasheet
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Dynein light chain 1, Cytoplasmic domain (DYNLL1)

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