Recombinant Saccharomyces Cerevisiae Heat Shock Protein Ssa1 (SSA1) Protein (His&Myc)

Name: Recombinant Saccharomyces Cerevisiae Heat Shock Protein Ssa1 (SSA1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03895P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Saccharomyces Cerevisiae Heat Shock Protein Ssa1 (SSA1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P10591
Target Symbol	SSA1
Synonyms	SSA1; YAL005C; Heat shock protein SSA1; Heat shock protein YG100
Species	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	ERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDTVTKKAEETISWLDSNTTASKEEFDDKLKELQDIANPIMSKLYQAGGAPGGAAGGAPGGFPGGAPPAPEAEGPTVEEVD
Expression Range	443-642aa
Protein Length	Partial
Mol. Weight	28.3 kDa
Research Area	Cancer
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	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.
Subcellular Location	Cytoplasm. Secreted, cell wall.
Protein Families	Heat shock protein 70 family
Database References	KEGG: sce:YAL005C STRING: 4932.YAL005C

Gene Functions References

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
Studied deletions of two major chaperone proteins, SSA1 and SSB1, from the HSP70 chaperone network in Sacchromyces cerevisiae. PMID: 25689132
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
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
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
Ssa1p and Swa2p cooperatively disassemble yeast clathrin coat baskets PMID: 23913685
The Hsp70 Chaperone Ssa1 and the AAA-Type ATPase Cdc48 Are Required for Ubr1-Dependent ERAD of Ste6*. PMID: 23988329
Data indicate that the Hsp70, Ssa1p, facilitates an interaction between a novel misfolded substrate and San1p. PMID: 23653356
Sis1 and Hsp70 operate sequentially with the quality control E3 ubiquitin ligase Ubr1 to target short-lived green fluorescent protein for degradation. PMID: 23341891
findings demonstrate that Hsp70 is a proximal sensor for Hsf1-mediated cytoprotection and can discriminate between two distinct environmental stressors PMID: 22809627
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
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
a role for Ssa1 in mediating localization of nascent peptide-ribosome-mRNA complexes to the mitochondria PMID: 22138184
Conformation-dependent Ssa1 hydrophobicity and aggregation play a key role in Ssa1 function. PMID: 20835845
observations strongly suggest that lysine 339 and its flanking amino acid stretches are involved in the interaction between Ure2p and Ssa1p PMID: 21078122
Ssa1 plays a general role in elimination of gluconeogenic enzymes. PMID: 20513352
a potent cochaperone of Ssa1 is Cns1 PMID: 15044454
Stimulates prion formation and polymer growth by stabilizing misfolded proteins. PMID: 15545639
Sis1 has a bipartite interaction with Ssa in vivo PMID: 15687271
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
characterized the influence of Hsp104 and Ssa1 on the disassembly of Hsp26 x substrate complexes in vitro and in vivo PMID: 15843375
SSB/SSE and SSA/SSE transiently associate with newly synthesized polypeptides with different kinetics PMID: 16219770
Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb PMID: 16221677
A structural basis for the regulation of heat-shock proteins in S. cerevisiae is presented. PMID: 16737444
The introduction of Ssa1p improves secretory proteins in Pichia pastoris secretion 4-7 times. PMID: 16889384
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
Stability experiments revealed that only Hsp70 proteins Ydj1-protected can hydrolyze ATP under prolonged stress. PMID: 17985367
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
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
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
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

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.