KDELR1 / ATTO 700 / 20000000.0
Product Details
| Description | Mouse monoclonal to HDEL (ATTO 700). HSP 70 family comprises four highly conserved proteins, HSP 70, HSC 70, GRP 75 and GRP 78, which serve a variety of roles. They act as molecular chaperones, facilitating the assembly of multi-protein complexes; participate in the translocation of polypeptides across cell membranes and to the nucleus; and aid in the proper folding of nascent polypeptide chains. GRP 78 is localized in the endoplasmic reticulum (ER), where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually KDEL in animal cells, and HDEL in S. cerevisiae. The 2E7 clone recognizes the C-terminal peptide HDEL, a common version of the endoplasmic reticulum retention signal found in yeast, plant, nematode and other ER proteins. 2E7 specifically stains HDEL proteins in barnyard grass, beet, cotton, mung bean, sorghum and wheat.. | |
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| Conjugate | ATTO 700 | |
| Clone | 20000000.0 | |
| Target Species | Drosophila, Saccharomyces, Yeast | |
| Applications | IF, ICC, WB | |
| Supplier | Biorbyt | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About KDELR1
Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, which is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and functionally similar to the yeast ERD2 gene product. [provided by RefSeq, Jul 2008]
Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, which is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and functionally similar to the yeast ERD2 gene product. [provided by RefSeq, Jul 2008]
About ATTO 700
ATTO 700 from ATTO-Tec Gmbh has an excitation peak at 700 nm and an emission peak at 719 nm.
ATTO 700 from ATTO-Tec Gmbh has an excitation peak at 700 nm and an emission peak at 719 nm.
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