CRNN Human

Cornulin Human Recombinant
Cat. No.
BT2679
Source
Escherichia Coli.
Synonyms
SEP53, DRC1, PDRC1, Cornulin, Tumor-related protein, Squamous epithelial heat shock protein 53, 53 kDa squamous epithelial-induced stress protein, 58 kDa heat shock protein, 53 kDa putative calcium-binding protein, CRNN, C1orf10.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 85% 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

CRNN Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 515 amino acids (1-495 a.a.) and having a molecular mass of 55.7 kDa. The CRNN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
CRNN, short for SEP53, belongs to a family of proteins characterized by a fusion of specific domains. These proteins possess N-terminal EF-hand domains, known for calcium binding, and multiple repeating peptide sequences. CRNN itself contains two of these EF-hand domains and two 60-amino acid repeats rich in glutamine and threonine at its C-terminus. Functionally, CRNN plays a role in both the immune response at mucosal and epithelial surfaces and in the differentiation of epidermal cells. Furthermore, CRNN acts as a survival factor, contributing to the ability of squamous esophageal epithelium cells to form colonies. It mitigates cell death and calcium release induced by deoxycholic acid (DCA). Interestingly, high levels of CRNN in oral squamous carcinoma cell lines can actually suppress cell proliferation by triggering G1 arrest.
Description
This product consists of the recombinant human CRNN protein, expressed in E. coli bacteria. A 20-amino acid Histidine tag is attached to the protein's N-terminal end to facilitate purification. This protein is a single, non-glycosylated polypeptide chain comprising 515 amino acids (specifically, amino acids 1 through 495). It has a molecular weight of 55.7 kDa. Purification of the CRNN protein is achieved using proprietary chromatographic methods, ensuring high purity.
Physical Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.
Formulation
The CRNN protein is supplied in a solution containing 20mM Tris-HCl buffer at a pH of 8 and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be kept at a refrigerated temperature of 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein (either 0.1% HSA or BSA) to the solution. Repeated freezing and thawing of the product should be avoided.
Purity
Analysis by SDS-PAGE confirms that the purity of this product exceeds 85%.
Synonyms
SEP53, DRC1, PDRC1, Cornulin, Tumor-related protein, Squamous epithelial heat shock protein 53, 53 kDa squamous epithelial-induced stress protein, 58 kDa heat shock protein, 53 kDa putative calcium-binding protein, CRNN, C1orf10.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPQLLQNING IIEAFRRYAR TEGNCTALTR GELKRLLEQE FADVIVKPHD PATVDEVLRL LDEDHTGTVE FKEFLVLVFK VAQACFKTLS ESAEGACGSQ ESGSLHSGAS QELGEGQRSG TEVGRAGKGQ HYEGSSHRQS QQGSRGQNRP GVQTQGQATG SAWVSSYDRQ AESQSQERIS PQIQLSGQTE QTQKAGEGKR NQTTEMRPER QPQTREQDRA HQTGETVTGS GTQTQAGATQ TVEQDSSHQT GRTSKQTQEA TNDQNRGTET HGQGRSQTSQ AVTGGHAQIQ AGTHTQTPTQ TVEQDSSHQT GSTSTQTQES TNGQNRGTEI HGQGRSQTSQ AVTGGHTQIQ AGSHTETVEQ DRSQTVSHGG AREQGQTQTQ PGSGQRWMQV SNPEAGETVP GGQAQTGAST EPGRQEWSST HPRRCVTEGQ GDRQPTVVGE EWVDDHSRET VILRLDQGNL HTSVSSAQGQ DAAQSEEKRG ITARELYSYL RSTKP.

Product Science Overview

Structure and Function

Cornulin contains several key structural domains:

  • N-terminus EF-hand domains: These are calcium-binding motifs that play a crucial role in the protein’s function.
  • Two glutamine- and threonine-rich 60 amino acid repeats: Located in the C-terminus, these repeats are significant for the protein’s stability and function .

Cornulin is involved in various cellular processes, including:

  • Cell Proliferation: It promotes cell proliferation and the G1/S cell cycle progression by inducing the expression of the cell cycle regulator CCND1 .
  • Immune Response: It plays a role in the mucosal/epithelial immune response and epidermal differentiation .
  • Stress Response: Initially identified as a squamous epithelial heat shock protein, Cornulin is also known as a stress protein that responds to cellular stress conditions .
Expression and Clinical Significance

Cornulin is predominantly expressed in squamous epithelial tissues, such as the esophagus . Its expression is regulated by various factors, including pro-inflammatory cytokines, through the activation of NFKB1 and PI3K/AKT signaling pathways .

Clinically, Cornulin has been associated with several diseases:

  • Esophageal Cancer: Altered expression of Cornulin has been linked to the development and progression of esophageal cancer .
  • Squamous Cell Carcinoma: It is also implicated in squamous cell carcinoma, highlighting its potential role as a biomarker for these cancers .
Recombinant Cornulin

Recombinant Human Cornulin is produced using Escherichia coli expression systems and is available for research purposes . This recombinant protein retains the full length of the human Cornulin protein and is used in various applications, including SDS-PAGE .

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