Recombinant Saccharomyces Cerevisiae Gtp-Binding Protein Ypt1 (YPT1) Protein (His)

Name: Recombinant Saccharomyces Cerevisiae Gtp-Binding Protein Ypt1 (YPT1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10534P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Saccharomyces Cerevisiae Gtp-Binding Protein Ypt1 (YPT1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P01123
Target Symbol	YPT1
Synonyms	YPT1; YP2; YFL038C; GTP-binding protein YPT1; Protein YP2; Rab GTPase YPT1; Transport GTPase YPT1
Species	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQIWDTAGQERFRTITSSYYRGSHGIIIVYDVTDQESFNGVKMWLQEIDRYATSTVLKLLVGNKCDLKDKRVVEYDVAKEFADANKMPFLETSALDSTNVEDAFLTMARQIKESMSQQNLNETTQKKEDKGNVNLKGQSLTNTGGGCC
Expression Range	1-206aa
Protein Length	Full Length
Mol. Weight	25.2kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. YPT1 regulates the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. Also involved in the recycling of membrane proteins.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cytoplasm. Preautophagosomal structure membrane; Lipid-anchor; Cytoplasmic side. Note=ER and Golgi when GTP-bound. Cytoplasmic when bound to GDI1.
Protein Families	Small GTPase superfamily, Rab family
Database References	KEGG: sce:YFL038C STRING: 4932.YFL038C

Gene Functions References

TRAPPIII and Ypt1 control membrane trafficking events under normal growth conditions and during autophagy. PMID: 29109089
Since these there proteinases belong to the CPY pathway, YPT1 is even believed to up-regulate this trafficking pathway in yeast cells. Future studies, however, should be carried out to discover the mechanisms that allow YPT1 to recruit these proteins into yeast vacuoles PMID: 26895320
that changes in Ypt1 and Ypt31 activity affect Golgi cisternal progression, early-to-transitional and transitional-to-late, respectively PMID: 26906739
Ypt1 binds and activates Hrr25 to spatially regulate its kinase activity. PMID: 26195667
Finally, three sequential steps of this pathway are delineated: Atg9-dependent exit from the ER en route to autophagy, Ypt1- and core Atgs-mediated pre-autophagsomal-structure organization, and Ypt51-mediated delivery of APs to the vacuole PMID: 26181331
results suggest that Ypt1p is involved in the cellular protection process under heat stress conditions PMID: 26169936
These findings establish a role for an autophagy-specific Ypt1 module in the regulation of ER-phagy. Moreover, because Ypt1 is a known key regulator of ER-to-Golgi transport, these findings establish a second role for Ypt1 at the ER PMID: 23924895
Findings show that Ypt1/Rab1 infindings show that Ypt1/Rab1 interacts with Atg1/Ulk1 in yeast and mammalian cells. PMID: 23716696
Trs85 and Ypt1 are localized to the preautophagosomal structure in an Atg9-dependent manner. PMID: 23129774
Our findings establish that Ypt1 contributes to regulation of UPR signaling dynamics by promoting the decay of HAC1 RNA, suggesting a potential regulatory mechanism for linking vesicle trafficking to the UPR and ER homeostasis PMID: 22844259
Ypt1 and Atg11 colocalize with Trs85, a Ypt1 activator subunit, and together they regulate selective autophagy. PMID: 22509044
Ypt1 is essential for autophagy. PMID: 20375281
alpha-Synuclein expression blocks ER-to-Golgi vesicular trafficking; in a genomewide screen, the largest class of toxicity modifiers were proteins functioning at this step including Ypt1p which associated with cytoplasmic alphaSyn inclusions PMID: 16794039
These results show that Trs65 plays a role in the Ypt guanine nucleotide exchanger activity of TRAPP II in concert with the two other TRAPP II-specific subunits. PMID: 17475775
These results confirm the link between translation and vesicular trafficking and reinforce the implication of eIF5A in protein synthesis. PMID: 18568365
Study presents the structure of a heteropentameric TRAPPI assembly complexed with Ypt1p & leads to proposal for mechanism for guanine nucleotide exchange in which each subunit in the TRAPPI subassembly contributes to the activity of this multimer. PMID: 18585354
identify the kinetic and thermodynamic bases by which TRAPP catalyzes nucleotide exchange from Ypt1p PMID: 19361519
Data show that Gyp1p, a GAP for Ypt1p, specifically interacts with Ypt32p, and that this interaction is important for the localization and stability of Gyp1p. PMID: 19666511

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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