CISD1 Human

CDGSH Iron Sulfur Domain 1 Human Recombinant
Cat. No.
BT30660
Source
E.coli.
Synonyms
CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

CISD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 100 amino acids (32-108) and having a molecular mass of 11.4 kDa.
CISD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
The CISD1 protein contains a CDGSH iron-sulfur domain and binds a redox-active [2Fe-2S] cluster. It is found exclusively in the outer mitochondrial membrane and plays a role in regulating oxidation.
Description
Recombinant human CISD1 protein was produced in E. coli. It is a single polypeptide chain consisting of 100 amino acids (residues 32-108) with a molecular weight of 11.4 kDa. The protein has a 23 amino acid His-tag attached to the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile filtered solution.
Formulation
The CISD1 protein solution is formulated in 20mM Tris-HCl buffer with a pH of 8.0, 0.15M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the CISD1 solution can be stored at 4°C. For longer-term storage, it is recommended to store the solution frozen at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Repeated freezing and thawing of the solution should be avoided.
Purity
The purity of the CISD1 protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKRFYVKD HRNKAMINLH IQKDNPKIVH AFDMEDLGDK AVYCRCWRSK KFPFCDGAHT KHNEETGDNV GPLIIKKKET

Product Science Overview

Introduction

The CDGSH Iron Sulfur Domain 1 (CISD1), also known as mitoNEET, is a protein that plays a crucial role in cellular iron metabolism and mitochondrial function. This protein is characterized by the presence of a CDGSH iron-sulfur binding domain, which is essential for its function.

Structure and Function

The CDGSH domain is a unique iron-sulfur binding motif that coordinates a [2Fe-2S] cluster. The domain is defined by the consensus sequence [C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H], where the CDGSH sequence is underlined, and the 3Cys-1His 2Fe-2S coordinating amino acids are indicated in bold . This domain was initially thought to be a zinc finger binding domain but was later shown to bind a 2Fe-2S iron-sulfur cluster .

CISD1 is an integral membrane protein located in the outer mitochondrial membrane. It functions as a homodimer and is involved in the regulation of iron and reactive oxygen metabolism . The protein is implicated in various physiological processes, including diabetes, obesity, cancer, cardiovascular disease, and neurodegeneration .

Evolutionary Background

The CDGSH domain is ancient in origin and appears in many important plant and animal proteins. It is believed to have appeared early in evolution, possibly linked to the heavy use of iron-sulfur driven metabolism by early organisms . The human CISD1 protein is thought to have originated from a mitochondrial endosymbiotic event .

Biological Significance

CISD1, along with other CDGSH proteins, plays a significant role in maintaining cellular iron homeostasis and protecting cells from oxidative stress. The protein’s ability to bind and transport iron is crucial for the function of several mitochondrial enzymes . Dysregulation of CISD1 has been associated with various diseases, including diabetes, cancer, and neurodegenerative disorders .

Research and Applications

Research on CISD1 has provided valuable insights into its structure, function, and evolutionary history. The protein’s role in disease mechanisms makes it a potential target for therapeutic interventions. Recombinant forms of CISD1 are used in research to study its function and to develop potential treatments for diseases associated with iron metabolism and mitochondrial dysfunction .

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