Analytical Data
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Gene name
ITIH4
- Application
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Alternative Names
ITIH4；IHRP；ITIHL1；PK120；Inter-alpha-trypsin inhibitor heavy chain H4
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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
Q14624
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Expression Region
689-930aa
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AA Sequence
RLAILPASAPPATSNPDPAVSRVMNMKIEETTMTTQTPAPIQAPSAILPLPGQSVERLCVDPRHRQGPVNLLSDPEQGVEVTGQYEREKAGFSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTGLLLLSDPDKVTIGLLFWDGRGEGLRLLLRDTDRFSSHVGGTLGQFYQEVLWGSPAASDDGRRTLRVQGNDHSATRERRLDYQEGPPGVEISCWSVEL
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Molecular Weight
42.9 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 ITIH4 (Inter-alpha-trypsin inhibitor heavy chain 4) protein is a member of the inter-alpha trypsin inhibitor family, which plays a crucial role in various physiological processes, including inflammation and tissue repair. Initially identified due to its involvement in the regulation of serine proteases, ITIH4 has garnered attention for its potential implications in pathological conditions such as cancer, cardiovascular diseases, and autoimmune disorders. Recent studies have highlighted its overexpression in certain malignancies, suggesting a role in tumor progression and metastasis. The unique properties of ITIH4, including its ability to form complexes with hyaluronic acid and its involvement in extracellular matrix organization, raise intriguing questions about its function in cellular signaling and the microenvironment. As a result, researchers are increasingly focused on characterizing the biochemical properties and clinical significance of ITIH4, especially in the context of therapeutic interventions and biomarker discovery. Understanding the structure-function relationship of ITIH4 and its interactions with other biomolecules may provide insights into novel strategies for disease management and highlight its potential as a target for therapeutic applications. Overall, the continued exploration of ITIH4 offers promising avenues for advancing medical science and improving patient outcomes in various diseases.
