Analytical Data
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Gene name
SERPINA3-5
- Application
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Alternative Names
SERPINA3-5；HTJ1；DnaJ homolog subfamily C member 1
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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
A2I7N1
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Expression Region
25-411aa
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AA Sequence
LPENVVVKDQRRRVDSHTLASSNTDFAFSLYKQLALKNPNKNVMFSPLSVSMALAFLSLGARGPTLTEILEGLKFNLTEIQETQIHQGFQHLLQALNRPSNQLQLSVGNAMFVQEELKLLDKFIEDARVLYSSEAFPTNFRDSEAARSLINDYVKNKTQGKIEELFKYLSPRTVLVLVNYIYFKAQWKTRFDPKHTEQAEFHVSKNKTVEVPMMTLDLETPYFRDKELGCMLVELTYSSNDSALFILPDEGKMQDLEAKLTPETLTRWRNSLQPRRIHELYLPKFSIKSNYELNDTLSQMGIKKIFTDADLSGITGTADLVVSQVVHGAALDVDEEGTEGAAATGIGIERTFLRIIVRVNRPFLIAVVLKDTQSIIFLGKVTNPSEA
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Molecular Weight
47.8 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
SERPINA3-5, a member of the serpin family of proteins, is primarily recognized for its role as a serine protease inhibitor, which is crucial in regulating various biological processes, including inflammation, cell proliferation, and apoptotic pathways. Research has increasingly focused on this protein due to its potential implications in several diseases, particularly in cancer and neurodegenerative disorders. Understanding the structure and function of SERPINA3-5 can provide insights into its regulatory mechanisms and interactions with other biomolecules. Recent studies have explored its expression patterns, revealing that SERPINA3-5 is often upregulated in pathological conditions, suggesting its involvement in disease progression and response to therapy. The study of recombinant SERPINA3-5 protein allows for the investigation of its functional properties in vitro and in vivo, providing a platform to examine its therapeutic potential. Furthermore, designing specific inhibitors or modulators targeting SERPINA3-5 could lead to novel treatment strategies for diseases where protease dysregulation is observed. Overall, the investigation into SERPINA3-5 reaffirms its significance in biomedical research, opening avenues for innovative therapeutic approaches in managing serious health conditions.
