Clusterin Human

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

1. Tiltle: Clusterin Facilitates Exchange of Glycosyl Phosphatidylinositol-Linked SPAM1 Between Reproductive Luminal Fluids and Mouse and Human Sperm Membranes1.
Publication:BIOLOGY OF REPRODUCTION 81, 562–570 (2009) Published online before print 8 April 2009. DOI 10.1095/biolreprod.108.075739
Link:Clusterin prospec publication

2. Tiltle: Mass spectrometry quantification of clusterin in the human brain.
Publication:2012 Chen et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the CreativeCommons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Link:Clusterin Human prospec publication

SDS

Clusterin Human Recombinant: Unraveling the Molecular Chaperone's Multifaceted Roles in Health and Disease

Abstract:

Clusterin, a versatile molecular chaperone, is involved in diverse physiological and pathological processes, making it an intriguing target for biomedical research. This paper provides a comprehensive analysis of Clusterin human recombinant, exploring its structure, functions, and potential applications. Understanding the intricacies of Clusterin sheds light on its significance in various biological contexts and highlights its potential as a therapeutic agent. This article offers a concise yet comprehensive examination of Clusterin, emphasizing its impact on human health.

Introduction:

The multifunctional protein Clusterin has emerged as a fascinating molecule with diverse roles in cellular homeostasis, neuroprotection, and tissue repair. This paper delves into the intricate nature of Clusterin, unveiling its structural features, molecular interactions, and involvement in various physiological processes.

Structure and Function of Clusterin:

Clusterin exhibits a complex structure, comprising multiple isoforms and domains that enable its interactions with a wide range of ligands. It functions as a molecular chaperone, aiding in protein folding, clearance of cellular debris, and regulation of apoptosis. Clusterin also plays a role in lipid transport and immune modulation.

Biological Implications of Clusterin:

Clusterin's involvement in diverse biological processes highlights its significance in health and disease. It contributes to the maintenance of tissue homeostasis, participates in neuroprotection, and influences immune responses. Moreover, Clusterin has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.

Clusterin Human Recombinant Production:

Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, allow for the production of Clusterin human recombinant. These methods facilitate large-scale production, purification, and characterization of Clusterin, offering opportunities for therapeutic applications.

Therapeutic Potential of Clusterin Human Recombinant:

Harnessing the therapeutic potential of Clusterin holds promise in various clinical scenarios. Its chaperone-like properties make it an attractive target for the development of therapies against protein misfolding diseases. Additionally, Clusterin's involvement in tissue repair and immune modulation opens avenues for therapeutic interventions in neurodegenerative diseases and cancer.

Conclusion:

Clusterin human recombinant represents a captivating field of research, unraveling the multifaceted roles of this molecular chaperone in health and disease. Understanding the structure, functions, and biological implications of Clusterin is essential in advancing our knowledge and exploring its potential therapeutic applications. Continued investigation into the mechanisms of Clusterin will likely pave the way for innovative therapeutic strategies in diverse fields of medicine.