CTF1 Human

Cardiotrophin-1 Human Recombinant
Cat. No.
BT19793
Source
Escherichia Coli.
Synonyms
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.
The CTF1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cardiotrophin 1 (CT-1), a member of the interleukin-6 superfamily, comprises 201 amino acids. Its discovery stemmed from its ability to induce a hypertrophic response in cardiac myocytes. CT-1 mRNA expression has been observed in both cardiac myocytes and non-myocytes. Significant CT-1 presence was also identified in healthy adult human lung tissue, with expression evident in both fetal and adult airway smooth muscle cells. CT-1 activates gp130-dependent signaling pathways, including the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway, to transmit hypertrophic and cytoprotective signals in cardiac myocytes. Beyond its cardiac role, CT-1 exhibits neurotrophic functions. CTF1 deficiency in mice leads to increased motoneuron cell death in the spinal cord and brainstem nuclei between embryonic day 14 and the first postnatal week. Furthermore, CT-1 acts as a hepatocyte survival factor, effectively mitigating hepatocellular damage in animal models of acute liver injury. CT-1 expression increases after hypoxic stimulation, offering cardioprotection when administered before simulated ischemia or during reoxygenation following simulated ischemia. This protective effect may stem from CT-1's ability to induce the expression of heat shock proteins (hsps) in cardiac cells. CT-1 also influences the ventricular expression of various factors. It increases the expression of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and angiotensinogen mRNA. Clinical studies have revealed elevated Cardiophin 1 levels in patients experiencing heart failure, dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina, and after acute myocardial infarction.
Description
Recombinant human Cardiotrophin-1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 201 amino acids, resulting in a molecular weight of 21.2 kDa. The purification of CTF1 is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
CTF-1 protein was lyophilized from a 0.2µm filtered solution containing 30% Acetonitrile and 0.1% TFA.
Solubility
To reconstitute the lyophilized CTF1, it is recommended to dissolve it in sterile 4mM HCl at a concentration of at least 100µg/ml. This solution can be further diluted into other aqueous solutions.
Stability
Lyophilized CTF1 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. Once reconstituted, CTF-1 should be stored at 4°C for 2-7 days. For extended storage, freezing at -18°C is advised. To ensure optimal stability during long-term storage, consider adding a carrier protein such as 0.1% HSA or BSA. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95.0%, as determined by the following methods: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED₅₀, as determined by a cell proliferation assay using human TF-1 cells, is less than 1.0 ng/ml. This corresponds to a specific activity of greater than 1.0 x 10⁶ IU/mg.
Synonyms
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
Source
Escherichia Coli.
Amino Acid Sequence
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

Product Science Overview

Structure and Source

CT-1 is a 201 amino acid protein with a molecular mass of approximately 21 kDa . The recombinant form of CT-1 is typically produced in Escherichia coli (E. coli) and is available in both glycosylated and non-glycosylated forms . The protein is often lyophilized and can be reconstituted in sterile solutions for various applications .

Biological Functions

CT-1 is a pleiotropic cytokine, meaning it has multiple effects on different cell types . It activates gp130-dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway . This signaling pathway is crucial for transducing hypertrophic and cytoprotective signals in cardiac myocytes . Additionally, CT-1 has neurotrophic functions and is involved in the survival of motoneurons .

Clinical Significance

CT-1 expression is augmented after hypoxic stimulation and can protect cardiac cells during ischemic events . It has been shown to induce the expression of protective heat shock proteins (hsps) in cardiac cells . Elevated levels of CT-1 have been observed in patients with heart failure, dilatative cardiomyopathy, mitral regurgitation, stable and unstable angina, and after acute myocardial infarction .

Applications

Recombinant human CT-1 is used in various research applications, including:

  • Cell Proliferation Assays: CT-1 is measured in cell proliferation assays using TF-1 human erythroleukemic cells .
  • Cardiac Research: Due to its role in inducing hypertrophic responses and protecting cardiac cells, CT-1 is extensively studied in cardiac research .
  • Neurobiology: CT-1’s neurotrophic functions make it a subject of interest in neurobiology research .
Storage and Stability

Recombinant CT-1 is typically stored at -20 to -70°C and should be reconstituted in sterile solutions containing human or bovine serum albumin to enhance stability . It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity .

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