DYNLL1 Human

Dynein Light Chain LC8 Type-1 Human Recombinant
Cat. No.
BT358
Source
Escherichia Coli.
Synonyms
PIN, DLC1, DLC8, DNCL1, DNCLC1, Dynein Light Chain LC8-type 1, Dynein Cytoplasmic Light polypeptide 1, Protein Inhibitor of Neuronal Nitric Oxide Synthase
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

DYNLL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a.) and having a molecular mass of 12.5kDa. The DYNLL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
DYNLL1, a protein interacting with NOS1, acts as an inhibitor of NOS1. This interaction disrupts the dimer conformation of NOS1 (Neuronal nitric oxide synthase) which is essential for its activity. By affecting nitric oxide synthase activity, DYNLL1 participates in the regulation of various biological processes. This ubiquitously expressed protein exhibits high expression levels in the testis and moderate levels in the brain.
Description
Recombinant Human DYNLL1, expressed in E.Coli, is a single, non-glycosylated polypeptide chain. It consists of 109 amino acids (1-89a.a.) and has a molecular weight of 12.5kDa. A 20 amino acid His-Tag is fused to the N-terminus of the DYNLL1 protein. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The DYNLL1 protein is provided as a solution at a concentration of 1mg/ml. It is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 1mM DTT, and 10% glycerol.
Purity
SDS-PAGE analysis indicates a purity exceeding 90%.
Stability

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 maintain product integrity, avoid repeated freeze-thaw cycles.

Synonyms
PIN, DLC1, DLC8, DNCL1, DNCLC1, Dynein Light Chain LC8-type 1, Dynein Cytoplasmic Light polypeptide 1, Protein Inhibitor of Neuronal Nitric Oxide Synthase
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG

Product Science Overview

Introduction

Dynein Light Chain LC8 Type-1 (DYNLL1) is a protein encoded by the DYNLL1 gene in humans. It is a component of the cytoplasmic dynein complex, which is a motor protein complex responsible for the retrograde transport of vesicles and organelles along microtubules .

Structure and Function

DYNLL1 is a small protein with a molecular weight of approximately 12.5 kDa . It is known for its role as a non-catalytic accessory component of the cytoplasmic dynein 1 complex. This complex is essential for intracellular transport and motility, linking dynein to cargos and adapter proteins that regulate dynein function .

Biological Role

DYNLL1 interacts with various proteins, including neuronal nitric oxide synthase (NOS1), where it acts as an inhibitor. By binding to NOS1, DYNLL1 destabilizes the NOS1 dimer, a conformation necessary for its activity. This interaction suggests that DYNLL1 may regulate numerous biological processes through its effects on nitric oxide synthase activity .

Expression and Localization

DYNLL1 is ubiquitously expressed in various tissues, with high expression levels in the testis and moderate expression in the brain . It is localized in the cytoplasm, nucleus, and secretory granules, and is part of the cytoplasmic dynein complex .

Recombinant Production

Recombinant human DYNLL1 protein, often fused to a His-tag at the N-terminus, is expressed in E. coli and purified using conventional chromatography techniques. The recombinant protein is used in various research applications to study its function and interactions .

Clinical Significance

Mutations or dysregulation of DYNLL1 have been associated with several diseases, including enterokinase deficiency and Bardet-Biedl syndrome . Its role in intracellular transport and nitric oxide synthase regulation makes it a critical protein for maintaining cellular homeostasis.

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