Clusterin Human

Clusterin Human Recombinant
Cat. No.
BT12736
Source
293 cell line (Human embryonic kidney).
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Appearance
Filtered, White, Lyophilized powder.
Purity
Greater than 95% 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

Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa.
Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Clusterin, also known as Apolipoprotein J (APO-J), is a 75-80 kDa heterodimeric protein composed of two disulfide-linked chains. It is heavily glycosylated, with approximately 30% of its mass consisting of N-linked carbohydrates rich in sialic acid. While the mature form is secreted, truncated versions targeted to the nucleus also exist. The protein is synthesized as a single polypeptide chain that undergoes proteolytic cleavage to remove a 22-amino acid signal peptide and further processing to generate the mature α and β chains. These chains associate in an anti-parallel manner, forming the heterodimer. The cysteine-rich centers of each chain are linked by five disulfide bridges and are flanked by predicted structural motifs including coiled-coil and amphipathic α-helices. Clusterin exhibits a high degree of evolutionary conservation, with 70% to 80% sequence homology across various species. It is widely expressed in mammalian tissues and is found in various bodily fluids such as plasma, milk, urine, cerebrospinal fluid, and semen. This protein interacts with a wide array of molecules including immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta-amyloid, and leptin. This promiscuous binding is reflective of its proposed involvement in a multitude of biological processes, including phagocyte recruitment, aggregation induction, complement regulation, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport, and scavenging. However, a definitive function for clusterin remains elusive. One prominent hypothesis suggests that clusterin acts as an extracellular chaperone, safeguarding cells against stress-induced damage caused by the accumulation of misfolded and aggregated proteins. Dysregulation of clusterin expression, both at the mRNA and protein levels, has been implicated in a wide range of pathological conditions, including cancer, organ regeneration, infection, Alzheimer's disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, and autoimmune disorders.
Description
Recombinant Human Clusterin is produced in HEK cells. It is a glycosylated polypeptide chain encompassing 438 amino acids with a molecular weight of 51.27 kDa. The protein consists of amino acids 1-427 of Clusterin and an 11 amino acid C-terminal flag tag. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
White, lyophilized powder (filtered).
Formulation
Lyophilized from a solution of phosphate-buffered saline (PBS) at pH 7.5 and filtered through a 0.4-micron filter.
Solubility
To prepare a working stock solution of approximately 0.5 mg/ml, reconstitute the lyophilized powder in deionized water. Allow sufficient time for the pellet to dissolve completely. Note: This product is not sterile. Before use in cell culture, it is essential to filter the reconstituted protein through an appropriate sterile filter.
Stability
The lyophilized protein should be stored at -20°C. Once reconstituted, aliquot the protein to minimize repeated freeze-thaw cycles. Reconstituted protein can be stored at 4°C for up to two weeks without any observable changes in stability.
Purity
Purity is determined to be greater than 95% as assessed by SDS-PAGE.
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Source
293 cell line (Human embryonic kidney).
Amino Acid Sequence
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

Product Science Overview

Introduction

Clusterin, also known as Apolipoprotein J, Sulfated Glycoprotein 2 (SGP-2), TRPM-2, and SP-40,40, is a secreted multifunctional protein that was named for its ability to induce cellular clustering . It is a glycoprotein with multiple biological functions and is involved in various physiological and pathological processes within the organism . Clusterin is predominantly expressed in adult testis, ovary, adrenal gland, liver, heart, and brain, and in many epithelial tissues during embryonic development .

Structure and Function

Clusterin is synthesized as a precursor that contains two coiled coil domains, three nuclear localization signals (NLS), and one heparin binding domain . It binds a wide range of molecules and may function as a chaperone of misfolded extracellular proteins . The protein is involved in processes such as regulating inflammation, controlling cell apoptosis, and clearing pathological proteins .

Role in Disease

Clusterin has attracted extensive research attention, particularly in Alzheimer’s disease (AD) research. It plays a significant role in the disease’s occurrence and progression. The expression level of Clusterin in the brain tissue of AD patients is closely related to pathological progression. Clusterin is involved in the deposition and formation of β-amyloid, which is a crucial process in AD development . Furthermore, Clusterin may affect the pathogenesis of AD through mechanisms such as regulating inflammation, controlling cell apoptosis, and clearing pathological proteins .

Recombinant Human Clusterin

Recombinant human Clusterin is produced using advanced biotechnological methods. It is typically derived from a mouse myeloma cell line, NS0, and is expressed as a disulfide-linked heterodimer . The recombinant protein is purified to a high degree, with a purity greater than 90% as determined by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining . The endotoxin level is kept below 1.0 EU per 1 μg of the protein by the LAL method .

Applications

Recombinant human Clusterin is used in various research applications, including studies on cell clustering, protein misfolding, and neurodegenerative diseases. It is also used as a potential therapeutic target in diseases such as Alzheimer’s disease .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.