Analytical Data
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Gene name
SIL1
- Application
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Alternative Names
SIL1;Nucleotide exchange factor SIL1
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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
Q9H173
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Expression Region
32-461aa
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AA Sequence
MHQNLKEFAL TNPEKSSTKE TERKETKAEE ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL RLEHHHHHH
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Molecular Weight
50 kDa
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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
SIL1 (Silderenase 1) is a crucial protein implicated in the process of protein folding and maturation within the endoplasmic reticulum (ER). As a co-chaperone of the Heat Shock Protein 70 (HSP70) family, SIL1 plays an essential role in assisting the folding of newly synthesized proteins and in the quality control of the intracellular environment. Genetic mutations in the SIL1 gene are associated with the rare autosomal recessive disorder known as MILS (Myeloid Leukemia with Intrauterine Growth Restriction and Liver Dysfunction). Research into SIL1’s functions is vital for understanding its contribution to cellular health and the consequences of its dysfunction, which can lead to severe pathological conditions. Studies have demonstrated that SIL1 enhances the activity of HSP70, thereby facilitating the proper folding of client proteins and mitigating ER stress. Furthermore, SIL1's interactions with other molecular chaperones highlight its integral role in maintaining protein homeostasis. Investigating the structure and function of SIL1 can provide insights into the mechanisms of ER-associated diseases and may aid in the development of targeted therapies for conditions arising from chaperone dysfunctions. Overall, the study of SIL1 is critical not only for elucidating the molecular basis of related diseases but also for advancing therapeutic approaches in biomedical research.
