DYNLL2 Human

Dynein Light Chain LC8 Type-2 Human Recombinant
Cat. No.
BT414
Source
Escherichia Coli.
Synonyms
Dynein light chain LC8-type 2, DNCL1B, Dlc2, MGC17810, RSPH22, 8kDa dynein light chain b, DLC8b, dynein light chain 2 cytoplasmic, radial spoke 22 homolog.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's 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

DYNLL2 Human Recombinant 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.
DYNLL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Dyneins are complex, high-molecular-weight ATPases that work with microtubules to convert the chemical energy stored in ATP into mechanical energy for movement. DYNLL2, a large protein complex with six distinct subunits, plays a crucial role in numerous intracellular movements towards the minus ends of microtubules. This highly conserved eukaryotic protein acts as a central hub, interacting with numerous binding partners and performing various functions beyond its role as a subunit of dynein and myosin Va motor proteins.
Description
Recombinant human DYNLL2, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 109 amino acids (1-89a.a) with a molecular weight of 12.5kDa. The protein is expressed with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The DYNLL2 protein solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 30% glycerol, 0.2M NaCl, and 1mM DTT.
Stability
For short-term storage, DYNLL2 remains stable at 4°C for up to one week. However, for long-term storage, it is recommended to store the protein below -18°C. Repeated freezing and thawing of the protein should be avoided.
Purity
The purity of DYNLL2 is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms
Dynein light chain LC8-type 2, DNCL1B, Dlc2, MGC17810, RSPH22, 8kDa dynein light chain b, DLC8b, dynein light chain 2 cytoplasmic, radial spoke 22 homolog.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG

Product Science Overview

Introduction

Dynein Light Chain LC8 Type-2 (DYNLL2) is a protein encoded by the DYNLL2 gene in humans. It is a part of the dynein motor protein complex, which is essential for various cellular processes, including intracellular transport, cell division, and ciliary function .

Structure and Function

DYNLL2 is a small protein, consisting of 89 amino acids, and shares a high degree of similarity with its paralog, DYNLL1 . It acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex. This complex functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules .

The primary role of DYNLL2 is to link dynein to its cargo and adapter proteins, thereby regulating dynein function. It is involved in various cellular pathways, including mitotic spindle formation and transport to the Golgi apparatus .

Biological Significance

DYNLL2 plays a crucial role in maintaining the spatial distribution of cytoskeletal structures. It is predicted to enable dynein intermediate chain binding activity and dynein light intermediate chain binding activity . Additionally, it is involved in cilium assembly and is active in glutamatergic synapses and postsynapses .

Recombinant DYNLL2

Recombinant DYNLL2 is produced using recombinant DNA technology, which involves cloning the DYNLL2 gene into an expression vector, transforming it into a suitable host cell (such as E. coli), and purifying the expressed protein. This recombinant protein is used in various research applications to study its function and interactions with other proteins.

Research Applications

Research on DYNLL2 has provided insights into its role in mitochondrial mobility within axons. For instance, studies have shown that DYNLL2 regulates syntaphilin-mediated mitochondrial docking in axons by binding to syntaphilin, thus enhancing the syntaphilin-microtubule docking interaction . This interaction is crucial for proper transport and distribution of mitochondria within neurons, which is essential for neuronal function .

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