- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-785
Synonyms
APOL-IV, APOLIV, Apolipoprotein L4, ApoL-IV.
Introduction
Apolipoprotein L 4 (APOL4) belongs to the apolipoprotein L family. APOL4 plays a role in lipid exchange and transport through the body, in addition to reverse cholesterol transport from peripheral cells to the liver. Two transcript variants encoding two different isoforms have been found for this gene. APOL4 is highly expressed in spinal cord, placenta, adrenal gland; also detected in spleen, bone marrow, uterus, trachea, mammary gland and testis
Description
APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348 a.a.) and having a molecular mass of 41.1kDa.
APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile filtered colorless solution.
Formulation
APOH protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Safety Data Sheet
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSMGSWVQL ITSVGVQQNH PGWTVAGQFQ EKKRFTEEVI EYFQKKVSPV HLKILLTSDE AWKRFVRVAE LPREEADALY EALKNLTPYV AIEDKDMQQK EQQFREWFLK EFPQIRWKIQ ESIERLRVIA NEIEKVHRGC VIANVVSGST GILSVIGVML APFTAGLSLS ITAAGVGLGI ASATAGIASS IVENTYTRSA ELTASRLTAT STDQLEALRD ILRDITPNVL SFALDFDEAT KMIANDVHTL RRSKATVGRP LIAWRYVPIN VVETLRTRGA PTRIVRKVAR NLGKATSGVL VVLDVVNLVQ DSLDLHKGAK SESAESLRQW AQELEENLNE LTHIHQSLKA G.
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Background
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.