CUTA Human

CutA Divalent Cation Tolerance Homolog Human Recombinant
Cat. No.
BT3444
Source
Escherichia Coli.
Synonyms
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek'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.
Shipped with Ice Packs
In Stock

Description

CUTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (33-179 a.a.) and having a molecular mass of 17.1 kDa. CUTA protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

Product Specs

Introduction
CUTA, the mammalian counterpart of the E. coli cutA protein, consists of 179 amino acids. Found ubiquitously, especially in brain tissue, CUTA plays a role in enabling cells to tolerate a wide array of divalent cations, excluding copper. This cytoplasmic protein is encoded by a single-gene operon.
Description
Recombinant Human CUTA, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 156 amino acids (spanning from amino acid 33 to 179). With a molecular weight of 17.1 kDa, this protein is fused with an 8 amino acid His-Tag at its C-terminus and is purified using standard chromatography techniques.
Physical Appearance
A colorless solution that has been sterilized through filtration.
Formulation
Human CUTA solution formulated in a buffer containing 20mM Tris-HCl at a pH of 8, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For longer periods, store frozen at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeding 95% as determined by SDS-PAGE analysis.
Synonyms
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
Source
Escherichia Coli.
Amino Acid Sequence
MRLLLLPRVL LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL QWVRQVTESV SDSITVLPLE HHHHHH.

Product Science Overview

Gene and Protein Structure

The CUTA gene is located on chromosome 6 at the cytogenetic location 6p21.32 . The gene encodes a protein that consists of 179 amino acids and has a molecular mass of approximately 14 kDa . The protein has several important structural features, including:

  • An N-terminal transmembrane domain
  • Three N-glycosylation sites
  • Two myristoylation sites
  • A glycosaminoglycan-binding site
  • Several phosphorylation sites
Function and Localization

CUTA is ubiquitously expressed in various tissues, with particularly high expression in the brain . The protein is involved in cellular copper sensitivity and the processing and trafficking of membrane proteins . It may form part of a complex of membrane proteins attached to acetylcholinesterase (AChE), an enzyme that degrades acetylcholine .

Role in Disease

Mutations or dysregulation of the CUTA gene have been associated with certain diseases, including Rhizomelic Chondrodysplasia Punctata, Type 3, and Chondrodysplasia Punctata Syndrome . These conditions are characterized by skeletal abnormalities and other developmental issues.

Research and Applications

Recombinant human CUTA protein is used in various research applications to study its function and role in disease. The protein’s ability to tolerate a broad range of divalent cations makes it a valuable tool for understanding cellular metal ion homeostasis .

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