Analytical Data
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Gene name
HSPC196
- Application
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Alternative Names
TMEM138; HSPC196; HSPC198; Transmembrane protein 138
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NPI0
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Expression Region
1-162aa
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AA Sequence
MLQTSNYSLVLSLQFLLLSYDLFVNSFSELLQKTPVIQLVLFIIQDIAVLFNIIIIFLMFFNTFVFQAGLVNLLFHKFKGTIILTAVYFALSISLHVWVMNLRWKNSNSFIWTDGLQMLFVFQRLAAVLYCYFYKRTAVRLGDPHFYQDSLWLRKEFMQVRR
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Molecular Weight
43.56 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
HSPC196, a member of the heat shock protein family, is gaining attention in the field of molecular biology due to its potential roles in cellular stress response and protein folding. Heat shock proteins are essential chaperones that assist in the proper folding and unfolding of proteins, protecting cells from stress-induced damage. Recent studies have suggested that HSPC196 might be involved in various cellular processes, including apoptosis, cell differentiation, and immune responses. Notably, its upregulation has been observed in several pathological conditions, including cancer and neurodegenerative diseases, indicating its possible role as a biomarker for disease progression or a target for therapeutic interventions. Additionally, research has focused on the recombinant production of HSPC196 to facilitate structure-function studies and to explore its interactions with other cellular proteins. Understanding the precise biological functions and mechanisms of action of HSPC196 could provide valuable insights into its potential applications in disease treatment and prevention, making it an important subject of investigation in both fundamental and applied research contexts.











