HSP12
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Official Full Name
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Overview
sHsps have some structural features in common: Very characteristic is a homologous and highly conserved amino acid sequence, the so-called α-crystallin-domain at the C-terminus. These sequences consist of 80 to 100 residues with a homology between 20% and 60% and form β-sheets, which are important for the formation of stable dimers. -
Synonyms
Hsp12p;HSP12;GLP1;HOR5;Plasma membrane localized protein that protects membranes from desiccation;induced by heat shock, oxidative stress, osmostress, stationary phase entry, glucose depletion, oleate and alcohol;regulated by the HOG and Ras-Pka pathways
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| HSP12-2136Y | Recombinant Yeast Hsp12p | E.coli | Yeast | Non |
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Involved Pathway
HSP12 involved in several pathways and played different roles in them. We selected most pathways HSP12 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with HSP12 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
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Protein Function
HSP12 has several biochemical functions, for example, lipid binding. Some of the functions are cooperated with other proteins, some of the functions could acted by HSP12 itself. We selected most functions HSP12 had, and list some proteins which have the same functions with HSP12. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| lipid binding | LIPF,APOA4B.2,INPP4B,EPN1,CRABP2A,STARD10,BPIFA5,Fert2,VCP,ACBD6 |
Interacting Protein
HSP12 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HSP12 here. Most of them are supplied by our site. Hope this information will be useful for your research of HSP12.
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