Recombinant Saccharomyces cerevisiae Heat shock protein SSA1 (SSA1), partial

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中文名稱：

釀酒酵母SSA1重組蛋白
貨號：

CSB-EP319915SVG
規格：

￥1836
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP319915SVG could indicate that this peptide derived from E.coli-expressed Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SSA1.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP319915SVG could indicate that this peptide derived from E.coli-expressed Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SSA1.
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靶點詳情

產品詳情

純度：

Greater than 85% as determined by SDS-PAGE.
基因名：

SSA1
Uniprot No.：

P10591
別名：

SSA1; YAL005C; Heat shock protein SSA1; Heat shock protein YG100
種屬：

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
蛋白長度：

Partial
來源：

E.coli
分子量：

28.3 kDa
表達區域：

443-642aa
氨基酸序列

ERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDTVTKKAEETISWLDSNTTASKEEFDDKLKELQDIANPIMSKLYQAGGAPGGAAGGAPGGFPGGAPPAPEAEGPTVEEVD
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
蛋白標簽：

N-terminal 10xHis-tagged and C-terminal Myc-tagged
產品提供形式：

Liquid or 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.
緩沖液：

Tris-based buffer，50% glycerol
儲存條件：

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

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.
貨期：

3-7 business days
注意事項：

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

Please contact us to get it.

產品評價

靶點詳情

功能：

May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
基因功能參考文獻：
1. Hsp90 (Hsp82) and yeast Hsp70 (Ssa1), directly interact in vitro in the absence of the yeast Hop homolog (Sti1), and identify a region in the middle domain of yeast Hsp90 that is required for the interaction. PMID: 29463764
2. Studied deletions of two major chaperone proteins, SSA1 and SSB1, from the HSP70 chaperone network in Sacchromyces cerevisiae. PMID: 25689132
3. yeast expressing P417L or P417S as the only copy of Ssa were temperature sensitive and exhibited defects in Ssa1-dependent protein translocation and misfolded protein degradation. PMID: 25913688
4. Nearly all interactions remained unchanged or decreased after DNA damage, but 5 proteins increased interactions with Ssa1 and/or Hsp82, including the ribonucleotide reductase (RNR) subunit Rnr4. PMID: 25452130
5. The major ubiquitin ligase targeting the superfluous Fas2 subunit to the proteasome is Ubr1. The ubiquitin-conjugating enzymes Ubc2 and Ubc4 assist the degradation process. PMID: 25564609
6. Ssa1p and Swa2p cooperatively disassemble yeast clathrin coat baskets PMID: 23913685
7. The Hsp70 Chaperone Ssa1 and the AAA-Type ATPase Cdc48 Are Required for Ubr1-Dependent ERAD of Ste6*. PMID: 23988329
8. Data indicate that the Hsp70, Ssa1p, facilitates an interaction between a novel misfolded substrate and San1p. PMID: 23653356
9. Sis1 and Hsp70 operate sequentially with the quality control E3 ubiquitin ligase Ubr1 to target short-lived green fluorescent protein for degradation. PMID: 23341891
10. findings demonstrate that Hsp70 is a proximal sensor for Hsf1-mediated cytoprotection and can discriminate between two distinct environmental stressors PMID: 22809627
11. T36 phosphorylation triggers displacement of Ydj1, allowing Ssa1 to bind the G1 cyclin Cln3 and promote its degradation; these results establish an active role for Hsp70 chaperones as signal transducers mediating growth control of G1 cyclin abundance and activity. PMID: 23217712
12. the client binding domain of Hsc70 and Ssa1p binds two regions within alpha-Syn similar to a tweezer, with the first spanning residues 10-45 and the second spanning residues 97-102. PMID: 22843682
13. a role for Ssa1 in mediating localization of nascent peptide-ribosome-mRNA complexes to the mitochondria PMID: 22138184
14. Conformation-dependent Ssa1 hydrophobicity and aggregation play a key role in Ssa1 function. PMID: 20835845
15. observations strongly suggest that lysine 339 and its flanking amino acid stretches are involved in the interaction between Ure2p and Ssa1p PMID: 21078122
16. Ssa1 plays a general role in elimination of gluconeogenic enzymes. PMID: 20513352
17. a potent cochaperone of Ssa1 is Cns1 PMID: 15044454
18. Stimulates prion formation and polymer growth by stabilizing misfolded proteins. PMID: 15545639
19. Sis1 has a bipartite interaction with Ssa in vivo PMID: 15687271
20. Data suggest that Ssa1-21p interferes with disruption of large Sup35p aggregates, which lack or have limited capacity to function as seed, into polymers that function more efficiently as [PSI+] seeds. PMID: 15701791
21. characterized the influence of Hsp104 and Ssa1 on the disassembly of Hsp26 x substrate complexes in vitro and in vivo PMID: 15843375
22. SSB/SSE and SSA/SSE transiently associate with newly synthesized polypeptides with different kinetics PMID: 16219770
23. Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb PMID: 16221677
24. A structural basis for the regulation of heat-shock proteins in S. cerevisiae is presented. PMID: 16737444
25. The introduction of Ssa1p improves secretory proteins in Pichia pastoris secretion 4-7 times. PMID: 16889384
26. Jjj1, when overexpressed, is able to partially substitute for the Zuo1:Ssb chaperone machinery by recruiting Ssa to the ribosome, facilitating its interaction with nascent polypeptide chains PMID: 17242366
27. Stability experiments revealed that only Hsp70 proteins Ydj1-protected can hydrolyze ATP under prolonged stress. PMID: 17985367
28. To determine how the mutations alter Hsp70 we analyzed biochemically the substrate-binding domain (SBD) mutant L483W and the nucleotide-binding domain (NBD) mutants A17V and R34K. PMID: 18706386
29. Sse1 exploits a Bag-1-like mechanism to catalyze nucleotide release, which involves opening of the Ssa1 NBD by tilting lobe II. Hsp110 proteins use a unique binding mode to catalyze nucleotide release from Hsp70s by a functionally convergent mechanism PMID: 18948593
30. These results suggest that cytosolic Hsp70 plays multiple roles in TBSV replication, such as affecting the subcellular localization and membrane insertion of the viral replication proteins as well as the assembly of the viral replicase. PMID: 19153242
31. An in vitro replicase assembly assay with Ssa1p(ts) revealed that functional Ssa1p is required during the replicase assembly process, but not during minus- or plus-strand synthesis of Tombusvirus. PMID: 19748649
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亞細胞定位：

Cytoplasm. Secreted, cell wall.
蛋白家族：

Heat shock protein 70 family
數據庫鏈接：

KEGG: sce:YAL005C

STRING: 4932.YAL005C