Analytical Data
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Gene name
PDIK1L
- Application
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Alternative Names
PDIK1L; CLIK1LSerine/threonine-protein kinase PDIK1L; EC 2.7.11.1; PDLIM1-interacting kinase 1-like
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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
Q8N165
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Expression Region
1-341 aa
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AA Sequence
MVSSQPKYDL IREVGRGSYG VVYEAVIRKT SARVAVKKIR CHAPENVELA LREFWALSSI KSQHPNVIHL EECILQKDGM VQKMSHGSNS SLYLQLVETS LKGEIAFDPR SAYYLWFVMD FCDGGDMNEY LLSRKPNRKT NTSFMLQLSS ALAFLHKNQI IHRDLKPDNI LISQTRLDTS DLEPTLKVAD FGLSKVCSAS GQNPEEPVSV NKCFLSTACG TDFYMAPEVW EGHYTAKADI FALGIIIWAM LERITFIDTE TKKELLGSYV KQGTEIVPVG EALLENPKME LLIPVKKKSM NGRMKQLIKE MLAANPQDRP DAFELELRLV QIAFKDSSWE T
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Molecular Weight
38.5 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
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Protein Description
PDIK1L, or Protein Disulfide Isomerase Family A Member 6 Like, has emerged as a significant focus in biochemical research due to its roles in cellular processes such as protein folding, endoplasmic reticulum (ER) stress response, and potential implications in cancer biology. This protein, a member of the protein disulfide isomerase family, is implicated in the formation and rearrangement of disulfide bonds in polypeptides, which is crucial for proper protein structure and function. The study of PDIK1L is particularly relevant in the context of diseases related to protein misfolding and aggregation, where its function could influence cellular homeostasis and survival. Recent findings suggest that PDIK1L may play a role in regulating apoptosis and the response to oxidative stress, making it a potential target for therapeutic intervention in various pathologies, including tumors. As researchers delve deeper into the molecular mechanisms of PDIK1L, there is an increasing interest in exploring its interactions with other molecular chaperones and its regulation under stress conditions. These insights could pave the way for novel strategies in dealing with diseases characterized by dysfunctional protein dynamics.
