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| Recombinant human Protein disulfide-isomerase protein |
| Product Name £º |
Recombinant human Protein disulfide-isomerase protein |
| Synonyms £º |
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| Catalog Number £º |
CSB-RP002544h |
| Relevance £º |
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP |
| Mol. Weight £º |
53 KD |
| Product Info £º |
GST tagged |
| Source £º |
E.coli derived |
| Purity £º |
95% |
| Image £º |
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| Storage Buffer £º |
PBS buffer£¬20mM GSH |
| Storage £º |
Store at -20¡æ, for extended storage, conserve at -20¡æ or -80¡æ. |
| Notes £º |
Repeated freezing and thawing is not recommended. Store working aliquots at 4¡æ for up to one week. |
| AA sequence £º |
LRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRG YPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDS AKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVI EFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLK KEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFE DVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPA SADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL-
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| Referrences £º |
[1] "Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene."
Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L., Koivu J., Kivirikko K.I.
EMBO J. 6:643-649(1987) [PubMed: 3034602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2] "The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum."
Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E., Merlino G.T., Pastan I.
J. Biol. Chem. 262:11221-11227(1987) [PubMed: 3611107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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