CRP (19-224 a.a) Human

c-Reactive Protein (19-224 a.a) Human Recombinant
Cat. No.
BT19251
Source
Escherichia Coli.
Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% 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

CRP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (19-224 a.a.) and having a molecular mass of 23.2kDa.
CRP is purified by proprietary chromatographic techniques.

Product Specs

Introduction
C-reactive protein (CRP) is an acute phase protein produced by the liver. Its levels rise significantly in response to inflammation. CRP serves as a general marker of inflammation, and its levels increase in conditions like infections, autoimmune disorders, and tissue injury. The protein is synthesized by hepatocytes, the main cells in the liver, stimulated by cytokines such as IL-1 and TNF alpha and beta. CRP levels can rise rapidly and dramatically, sometimes up to 1,000 times their normal level, making it a sensitive indicator of inflammation. It's important to note that CRP is a non-specific marker, meaning elevated levels don't pinpoint the exact cause or location of the inflammation. High CRP levels are associated with various conditions, including bacterial infections, rheumatoid arthritis, viral infections, transplant rejection, meningitis, heart attack, sepsis, bone infection (osteomyelitis), and others. Interestingly, CRP levels strongly correlate with Serum Amyloid A, another acute-phase protein.
Description
This product consists of the recombinant human CRP protein, specifically the amino acids 19 to 224. It is produced in E. coli bacteria and is a single, non-glycosylated polypeptide chain with a molecular weight of 23.2 kDa. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The CRP protein is supplied in a solution at a concentration of 1 mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0, contains 2M Urea as a denaturant, and 20% Glycerol as a stabilizer.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer-term storage, it is recommended to freeze the product at -20°C. Adding a carrier protein such as 0.1% HSA or BSA is advised for extended storage to prevent protein degradation. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the CRP protein is greater than 90.0%, as determined by SDS-PAGE, a standard method for analyzing protein purity.
Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Source
Escherichia Coli.
Amino Acid Sequence
MQTDMSRKAF VFPKESDTSY VSLKAPLTKP LKAFTVCLHF YTELSSTRGY SIFSYATKRQ DNEILIFWSK DIGYSFTVGG SEILFEVPEV TVAPVHICTS WESASGIVEF WVDGKPRVRK SLKKGYTVGA EASIILGQEQ DSFGGNFEGS QSLVGDIGNV NMWDFVLSPD EINTIYLGGP FSPNVLNWRA LKYEVQGEVF TKPQLWP.

Product Science Overview

Structure and Function

CRP is a pentameric protein found in the blood plasma, and it plays a pivotal role in the body’s immune response. It is produced by the liver in response to inflammation. The protein binds to phosphocholine expressed on the surface of dead or dying cells (and some types of bacteria) to activate the complement system via the C1Q complex. This process promotes phagocytosis by macrophages, thereby aiding in the clearance of necrotic and apoptotic cells.

Recombinant CRP (19-224 a.a)

The recombinant form of CRP, covering amino acids 19 to 224, is expressed in Escherichia coli and is a non-glycosylated polypeptide chain. This segment of CRP retains the biological activity of the full-length protein, making it suitable for various research applications. The recombinant protein is purified using advanced chromatographic techniques to ensure high purity and functionality .

Applications

Recombinant CRP is widely used in:

  • Biochemical assays: It serves as a standard or control in assays measuring CRP levels in biological samples.
  • Structural studies: Researchers use it to study the protein’s structure-function relationships.
  • Drug development: It is employed in screening potential therapeutic agents targeting inflammatory pathways.
Preparation and Purity

The preparation of recombinant CRP involves cloning the CRP gene into an expression vector, transforming E. coli cells, and inducing protein expression. The protein is then purified through a series of chromatographic steps, including ion exchange and size exclusion chromatography. The final product is typically greater than 95% pure, as confirmed by SDS-PAGE and HPLC analysis .

Importance in Research

The availability of high-quality recombinant CRP has significantly advanced our understanding of inflammation and its role in various diseases. It has enabled detailed studies on the protein’s interaction with other molecules, its role in the immune response, and its potential as a therapeutic target.

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