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Chaperones

Chaperones are molecular proteins that are found in the cytoplasm of cells particularly endoplasmic reticulum. All proteins exist as a chain of amino acids further folded into a tertiary structure. The function of chaperone proteins is to assist certain proteins into finding their correct three dimensional structure or unfolding into the more simple, chain of amino acids. Chaperone proteins can also assist in the assembly of folded subunit proteins into oligomeric structures. The assistance provided by chaperone proteins is necessary for many reasons. Some proteins form structures that are not covalently bonded. This means that certain environmental influences can denature these proteins. Heat, for instance, can cause proteins to become unfolded. Chaperones, then, help to keep the protein in its proper function. Another notable function of chaperone proteins is to insure that the protein has folded into the correct shape. Misfolded proteins can be repaired by chaperone proteins and thus, the chaperone is a very important part of the process of protein synthesis. The process by which chaperone proteins work differs depending on which type of chaperone protein is in question. There are basically 2 main times in which chaperones can act. They can act during translation and also after translation. This means that the amino acid chain can start to be folded as it is still being assembled, or it can be folded after its construction has completed. Misfolded proteins are the cause of many different disorders including degenerative diseases that occur as a result of aging.

Anti-calnexin antibody binds against target calnexin. Calnexin is localized in the endoplasmic reticulum membrane specifically in the melanosome. Calnexin is a calcium-binding protein that interacts with newly made proteins in the endoplasmic reticulum. Calnexin plays a chaperone role by assisting in the assembly of the protein and quality control in the endoplasmic reticulum by retaining the proteins that have been folded incorrectly. Anti-ERp29 antibody binds against ERp29 protein (chromosome 12 open reading frame 8). Chromosome 12 open reading frame 8 is localized in the endoplasmic reticulum of cells. ERp29 assists in the proper folding of proteins by allowing for post-translational modifications that are necessary for secretory proteins to be exported out of the endoplasmic reticulum. ERp29 is a recently categorized chaperone protein that can be up-regulated by the endoplasmic reticulum during times of cellular stress.

 
Product Number Title Applications Host Clonality
AC16-0011 Anti-P4HB Antibody WB Mouse Monoclonal (3-2B12)
AC16-0014 Anti-P4HB Antibody ELISA, WB, IHC(F), IHC(P), ICC, IF, FC Mouse Monoclonal (6-9H6)
AC16-0011-01 Anti-P4HB Antibody (AMCA) WB Mouse Monoclonal (3-2B12)
AC16-0011-02 Anti-P4HB Antibody (AP) WB Mouse Monoclonal (3-2B12)
AC16-0011-03 Anti-P4HB Antibody (APC) WB Mouse Monoclonal (3-2B12)
AC16-0011-04 Anti-P4HB Antibody (APC-Cy5.5) WB Mouse Monoclonal (3-2B12)
AC16-0011-05 Anti-P4HB Antibody (APC-Cy7) WB Mouse Monoclonal (3-2B12)
AC16-0011-06 Anti-P4HB Antibody (Avidin) WB Mouse Monoclonal (3-2B12)
AC16-0011-07 Anti-P4HB Antibody (Biotin) WB Mouse Monoclonal (3-2B12)
AC16-0011-08 Anti-P4HB Antibody (BPE) WB Mouse Monoclonal (3-2B12)
AC16-0011-09 Anti-P4HB Antibody (Cy3) WB Mouse Monoclonal (3-2B12)
AC16-0011-10 Anti-P4HB Antibody (Cy5) WB Mouse Monoclonal (3-2B12)