Analytical Data
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Gene name
ITIH5
- Application
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Alternative Names
ITIH5；KIAA1953；Inter-alpha-trypsin inhibitor heavy chain H5
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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
Q86UX2
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Expression Region
35-161aa
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AA Sequence
VPRQVRLLQRLKTKPLMTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIE FQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTTEENG EKGTEIFRASAVIPSKDKAAFFLSYEE
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Molecular Weight
31 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
The ITIH5 protein, a member of the inter-alpha-trypsin inhibitor (ITI) family, plays a significant role in various physiological processes, including inflammation, tissue repair, and extracellular matrix organization. This family of proteins is characterized by their ability to bind to hyaluronic acid and other components of the extracellular matrix, providing structural support and modulating cell behavior. Research into ITIH5 has garnered attention due to its potential implications in diseases such as cancer, cardiovascular disorders, and autoimmune conditions. Recent investigations have highlighted its involvement in regulating inflammatory responses, with evidence suggesting that altered ITIH5 expression may correlate with disease progression. Furthermore, the protein's unique structure and function present opportunities for therapeutic applications, such as targeted drug delivery systems and biomaterials for tissue engineering. As scientists continue to explore the precise mechanisms by which ITIH5 influences cellular processes, understanding its role in pathology could pave the way for novel diagnostic and therapeutic strategies, making it a promising subject for further biomedical research.
