UBQLN2 Human

Ubiquilin 2 Human Recombinant
Cat. No.
BT22977
Source
Escherichia Coli.
Synonyms
UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek'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

UBQLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 647 amino acids (1-624 a.a) and having a molecular mass of 68.1kDa. UBQLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ubiquilin-2, also known as UBQLN2, is a protein that plays a crucial role in the ubiquitin-proteasome system, which is responsible for degrading damaged or unnecessary proteins within cells. UBQLN2 contains two main domains: an N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. These domains allow UBQLN2 to interact with both proteasomes, the cellular machinery responsible for protein degradation, and ubiquitin ligases, enzymes that tag proteins for destruction. By linking these components, UBQLN2 facilitates the degradation of targeted proteins. Additionally, UBQLN2 has been found to bind to the ATPase domain of Stch, a protein similar to heat shock protein 70 (Hsp70). Mutations in the UBQLN2 gene have been linked to neurological disorders, including amyotrophic lateral sclerosis 15 (ALS 15), which may or may not be accompanied by frontotemporal dementia, a condition affecting the frontal and temporal lobes of the brain.
Description
Recombinant UBQLN2 protein, produced in E. coli bacteria, is a purified protein consisting of a single polypeptide chain that is not glycosylated (does not contain sugar modifications). It encompasses 647 amino acids, representing amino acids 1 through 624 of the full-length human UBQLN2 protein. The recombinant protein has a molecular weight of 68.1 kDa and includes a 23-amino acid His-tag attached to its N-terminus. This His-tag facilitates purification using specialized chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The UBQLN2 protein solution has a concentration of 0.25 mg/ml and is formulated in a buffer containing phosphate-buffered saline (pH 7.4), 20% glycerol, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the UBQLN2 protein solution should be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To further enhance stability during long-term storage, adding a carrier protein such as albumin (HSA or BSA) at a concentration of 0.1% is advisable. To maintain protein integrity, avoid repeated cycles of freezing and thawing.
Purity
The purity of the UBQLN2 protein is greater than 90%, as determined by SDS-PAGE analysis, a technique used to separate proteins based on their size.
Synonyms
UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAENGES SGPPRPSRGP AAAQGSAAAP AEPKIIKVTV KTPKEKEEFA VPENSSVQQF KEAISKRFKS QTDQLVLIFA GKILKDQDTL IQHGIHDGLT VHLVIKSQNR PQGQSTQPSN AAGTNTTSAS TPRSNSTPIS TNSNPFGLGS LGGLAGLSSL GLSSTNFSEL QSQMQQQLMA SPEMMIQIME NPFVQSMLSN PDLMRQLIMA NPQMQQLIQR NPEISHLLNN PDIMRQTLEI ARNPAMMQEM MRNQDLALSN LESIPGGYNA LRRMYTDIQE PMLNAAQEQF GGNPFASVGS SSSSGEGTQP SRTENRDPLP NPWAPPPATQ SSATTSTTTS TGSGSGNSSS NATGNTVAAA NYVASIFSTP GMQSLLQQIT ENPQLIQNML SAPYMRSMMQ SLSQNPDLAA QMMLNSPLFT ANPQLQEQMR PQLPAFLQQM QNPDTLSAMS NPRAMQALMQ IQQGLQTLAT EAPGLIPSFT PGVGVGVLGT AIGPVGPVTP IGPIGPIVPF TPIGPIGPIG PTGPAAPPGS TGSGGPTGPT VSSAAPSETT SPTSESGPNQ QFIQQMVQAL AGANAPQLPN PEVRFQQQLE QLNAMGFLNR EANLQALIAT GGDINAAIER LLGSQPS.

Product Science Overview

Introduction

Ubiquilin 2 (UBQLN2) is a protein encoded by the UBQLN2 gene in humans. It belongs to the ubiquilin family of proteins, which play a crucial role in the regulation of protein degradation within cells. Ubiquilin 2 is particularly significant due to its involvement in various cellular processes and its association with certain neurodegenerative diseases.

Structure and Function

Ubiquilin 2 contains two primary domains:

  1. N-terminal ubiquitin-like (UBL) domain: This domain is responsible for binding to the proteasome, a complex that degrades unneeded or damaged proteins.
  2. C-terminal ubiquitin-associated (UBA) domain: This domain binds to polyubiquitinated proteins, marking them for degradation.

These domains enable Ubiquilin 2 to act as a bridge between ubiquitinated proteins and the proteasome, facilitating the degradation of misfolded or damaged proteins .

Expression and Localization

Ubiquilin 2 is widely expressed in various tissues, including the brain, liver, and muscles. It is predominantly localized in the cytoplasm but can also be found in the nucleus and other cellular compartments .

Role in Neurodegenerative Diseases

Mutations in the UBQLN2 gene have been linked to familial amyotrophic lateral sclerosis (fALS) and frontotemporal dementia (FTD). These mutations result in the formation of a non-functional Ubiquilin 2 enzyme, leading to the accumulation of ubiquitinated proteins in motor neurons. This accumulation is believed to contribute to the neurodegenerative processes observed in these diseases .

Research and Therapeutic Potential

Research on Ubiquilin 2 has provided valuable insights into its role in protein homeostasis and neurodegeneration. Understanding the mechanisms by which Ubiquilin 2 functions and how its mutations lead to disease can pave the way for developing targeted therapies for ALS and FTD.

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