Analytical Data
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Gene name
P4Ha2
- Application
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Alternative Names
Procollagen-Proline,2-Oxoglutarate 4-Dioxygenase(Proline 4-Hydroxylase),Alpha Polypeptide II
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15460
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Expression Region
Ser27~Glu518
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Molecular Weight
43kDa
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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
P4Ha2, a member of the prolyl 4-hydroxylase family, plays a crucial role in collagen biosynthesis by catalyzing the hydroxylation of proline residues in collagen precursors, which is essential for the stability and functionality of the collagen triple helix. The study of P4Ha2 has garnered significant attention due to its involvement in various physiological processes and its implications in pathological conditions, including fibrosis, cancer, and other connective tissue disorders. Dysregulation of P4Ha2 activity has been linked to impaired collagen formation, leading to compromised structural integrity in tissues. Moreover, research has shown that P4Ha2 can influence cellular responses to hypoxia and play a role in the modulation of tumor microenvironments, making it a potential therapeutic target. Investigating the regulatory mechanisms of P4Ha2 expression and activity, as well as its interactions with other molecular pathways, offers promising avenues for developing novel strategies for treating diseases associated with collagen accumulation and degradation. Moreover, understanding P4Ha2's role in collagen metabolism could provide insights into aging-related changes in connective tissues, thus broadening the scope of its significance in both fundamental biology and clinical applications. This growing interest is reflected in the increasing number of studies aimed at elucidating the functional dynamics of P4Ha2, paving the way for innovative approaches in regenerative medicine and targeted therapies.
