Analytical Data
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Gene name
ST13
- Application
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Alternative Names
ST13;AAG2;FAM10A1;HIP;Hsc70-interacting Protein
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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
P50502
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Expression Region
1-369aa
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AA Sequence
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA
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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 ST13 protein, also known as ST13/CIOS1, has gained attention in recent years due to its critical roles in cellular stress responses and protein homeostasis. Emerging research highlights its involvement in the regulation of heat shock proteins (HSPs) and its function as a co-chaperone, which assists in protein folding and protects cells from misfolded proteins, thereby preventing apoptosis and maintaining cellular integrity. Additionally, ST13 has been implicated in various physiological processes, including cell proliferation and differentiation, suggesting its potential impact on development and disease mechanisms. Notably, dysregulation of ST13 expression has been observed in several cancers, indicating its possible role as a biomarker and therapeutic target. Moreover, ST13's interaction with multiple signaling pathways points towards its importance in various stress-related contexts, such as oxidative stress and endoplasmic reticulum stress. Consequently, the study of recombinant ST13 is crucial for elucidating its biological functions and therapeutic applications, as understanding its mechanisms may open new avenues for targeted treatments in diseases characterized by protein misfolding and cellular stress. The exploration of ST13 not only enhances our understanding of protein homeostasis but also holds promise for innovative strategies in combating various pathological conditions. As advancements in recombinant protein technology continue to improve the production and characterization of ST13, future studies could provide deeper insights into its roles in health and disease, paving the way for novel interventions in conditions associated with protein mismanagement and cellular stress response.
