Analytical Data
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Gene name
SGTA
- Application
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Alternative Names
SGTA;SGT;SGT1;Small glutamine-rich tetratricopeptide repeat-containing Protein alpha
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43765
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Expression Region
1-313aa
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AA Sequence
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR SRTPSASNDD QQE
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on SGTA (Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha) recombinant protein has gained significant attention due to its critical role in various cellular processes, including protein folding, stability, and degradation. SGTA is known to act as a co-chaperone of heat shock proteins, particularly Hsp70, assisting in the proper folding of nascent polypeptides and the refolding of denatured proteins. Beyond its chaperone functions, SGTA has been implicated in the regulation of cellular signaling pathways and the modulation of protein interactions, making it a potential target for therapeutic interventions. Additionally, abnormalities in SGTA expression or function have been linked to diverse diseases, including neurodegenerative disorders and cancers. To better understand its mechanisms and explore its therapeutic potential, researchers have been focusing on the production and characterization of recombinant SGTA proteins. Through techniques such as molecular cloning and protein expression systems, scientists aim to generate high-purity SGTA for functional assays, structural studies, and potential drug discovery. Investigating the properties and interactions of SGTA will provide invaluable insights into its biological roles and establish its relevance in health and disease, paving the way for novel therapeutic strategies.
