Recombinant Human Elastase-3B/CELA3B, N-His

Reference: YHC36701
Product nameRecombinant Human Elastase-3B/CELA3B, N-His
Uniprot IDP08861
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsElastase IIIB, Chymotrypsin-like elastase family member 3B, Elastase-3B, CELA3B, Protease E, ELA3B
ReferenceYHC36701
NoteFor research use only

Description of Recombinant Human Elastase-3B/CELA3B, N-His

Introduction to Recombinant Human Elastase-3B/CELA3B, N-His

Recombinant Human Elastase-3B/CELA3B, N-His is a protein that plays a crucial role in the degradation of elastin, a major component of the extracellular matrix in the human body. This protein is produced through the process of recombinant DNA technology, which involves inserting the gene responsible for producing elastase-3B into host cells, resulting in the production of large quantities of the protein. The N-His tag refers to a short amino acid sequence that is added to the protein during the production process, which allows for easy purification and identification of the protein.

Structure of Recombinant Human Elastase-3B/CELA3B, N-His

Recombinant Human Elastase-3B/CELA3B, N-His is a serine protease, meaning it belongs to a class of enzymes that use a serine residue in their active site to cleave peptide bonds. The protein is composed of 267 amino acids and has a molecular weight of approximately 30 kDa. It contains a signal peptide at the N-terminus, which is responsible for targeting the protein to the endoplasmic reticulum for proper folding and secretion. The N-His tag is located at the C-terminus of the protein and does not affect its enzymatic activity.

The three-dimensional structure of Recombinant Human Elastase-3B/CELA3B, N-His has been determined through X-ray crystallography, revealing a compact globular structure with a central catalytic domain and two flanking domains. The catalytic domain contains the active site where the serine residue is located, while the flanking domains are responsible for substrate binding and specificity.

Activity of this protein

Recombinant Human Elastase-3B/CELA3B, N-His is a potent enzyme that is involved in the breakdown of elastin, a fibrous protein that provides elasticity to tissues such as skin, lungs, and blood vessels. It does so by cleaving peptide bonds within the elastin protein, resulting in the fragmentation of the protein and loss of its structural integrity.

In addition to its role in elastin degradation, Recombinant Human Elastase-3B/CELA3B, N-His has also been found to have antibacterial properties. It is able to break down the cell walls of certain bacteria, making it a potential therapeutic agent for treating infections caused by these bacteria.

Application of Recombinant Human Elastase-3B/CELA3B, N-His

The main application of Recombinant Human Elastase-3B/CELA3B, N-His is in the field of drug development. It is considered a potential drug target for diseases associated with excessive elastin degradation, such as emphysema and aortic aneurysms. By inhibiting the activity of this protein, it is possible to slow down the degradation of elastin and potentially prevent or treat these diseases.

Recombinant Human Elastase-3B/CELA3B, N-His is also used in research studies to better understand its role in various biological processes. It is commonly used as a tool to study elastin degradation and its impact on different tissues and diseases. The N-His tag also allows for easy purification and detection of the protein in these studies.

In conclusion, Recombinant Human Elastase-3B/CELA3B, N-His is a crucial protein involved in the degradation of elastin and has potential applications in drug development and research. Its structure and activity have been extensively studied, making it a valuable tool for understanding the role of elastin in various diseases.

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