Anti-ERP57
535 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 894 - AB0004-200
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 600 µg
Parameters
| Additional information | Purification: Epitope affinity purified;Immunogen: Purified recombinante peptide derived from within residues 300 aa to the C-terminus of human ERP57 produced in E. coli.;Specificity test:Detects a band of 60 kDa by Western blot in the following canine, human, monkey, mouse, rat whole cell lysates.;Buffer: PBS, 20% glycerol and 0.05% sodium azide;References: Not yet referenced. |
|---|---|
| Storage and shipping | Store at -20 C for long-term storage. Store at 2-8 C for up to one month. |
AB0003-200
Anti-ERP57
Goat polyclonal to ERp57 - endoplasmic reticulum lumen marker. This endoplasmic reticulum protein interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. It has disulfide isomerase activity and complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
535 €
AB0003-500
Anti-ERP57
Goat polyclonal to ERp57 - endoplasmic reticulum lumen marker. This endoplasmic reticulum protein interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. It has disulfide isomerase activity and complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
782.5 €
AB0004-200
Anti-ERP57
Goat polyclonal to ERp57 - endoplasmic reticulum lumen marker. This endoplasmic reticulum protein interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. It has disulfide isomerase activity and complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
535 €
R1409-1
Anti-ERp72 Antibody
Protein disulfide isomerase or PDI is an enzyme in the endoplasmic reticulum in eukaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDI contains four thioredoxin-like domains, two of which retain the canonical CXXC motif. The reduced (that is, dithiol) form of PDI is able to catalyse a reduction of mispaired thiol residues of a particular substrate, acting as an isomerase. Another major function of PDI relates to its activity as a chaperone; i.e., it aids wrongly folded proteins to reach a correctly folded state without the aid of enzymatic disulfide shuffling. PDI helps load antigenic peptides into MHC class I molecules. These molecules (MHC I) are related to the peptide presentation by antigen-presenting cells in the immune response.
433.5 €
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