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Recombinant Saccharomyces cerevisiae Heat shock protein homolog SSE1 (SSE1), partial

Recombinant Saccharomyces cerevisiae Heat shock protein homolog SSE1 (SSE1), partial

Code	CSB-YP329183SVG
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Yeast
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Code	CSB-EP329183SVG
MSDS	MSDS Datasheet
Size	Pls inquire
Source	E.coli
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Code	CSB-EP329183SVG-B
MSDS	MSDS Datasheet
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP329183SVG
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP329183SVG
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

SSE1

Uniprot No.

P32589

Alternative Names

SSE1; MSI3; YPL106C; LPG3C; Heat shock protein homolog SSE1; Chaperone protein MSI3

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.

Gene References into Functions

The Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes. PMID: 28483531
13 novel mutations in Sse1 have varying effects on both the ability of S. cerevisiae to propagate the [PSI+] prion and also to grow at increased temperatures. PMID: 23797105
The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 is required for maintaining proper distribution of kinesin-5 motors within the spindle, which is subsequently required for bipolar spindle assembly in S phase. PMID: 22908312
Findings support a model in which Hsp110 chaperones control the fate of some client proteins by influencing the decision to fold or degrade as dictated by the Hsp70-Hsp90 chaperone environment. PMID: 20237159
The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A signaling. PMID: 15879503
Data suggest that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. PMID: 17923091
NEF activity of Sse1 requires nucleotide binding and let us propose a new model for Hsp110 function. PMID: 18218635
mechanistic model wherein Sse1 functionally partners with Hsp90 as an Hsp70 nucleotide exchange factor to promote client protein maturation and interaction with downstream effectors PMID: 18478233
The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported. PMID: 18550409
Data suggest that Sse1p does not employ the nucleotide-dependent allostery and peptide-binding mode of canonical Hsp70s, and that direct interactions of substrate with Sse1p may support Hsp70-assisted protein folding in a cooperative process. PMID: 18555782