Analytical Data
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Gene name
P4HTM
- Application
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Alternative Names
P4HTM；PH4；Transmembrane prolyl 4-hydroxylase
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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
Q9NXG6
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Expression Region
82-563aa
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AA Sequence
VHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRQVSPNWGLPSILRPGTPMTQAQPCTVGVPLGMGPGDHWVIPVSPWEHPQLGTCSVPPLPYSYMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREGGTDSQPEWALDRAYRDARVEL
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Molecular Weight
70.5 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
Related Products
Protein Description
P4HTM, or Prolyl 4-Hydroxylase Threonine-Methylated isoform, is a type of enzyme that plays a vital role in the post-translational modification of proteins through the hydroxylation of proline residues. This modification is crucial for stabilizing the triple-helix structure of collagen, which is indispensable in various biological processes, including tissue repair, cellular signaling, and maintaining extracellular matrix integrity. The study of P4HTM has garnered interest due to its implications in several diseases, such as fibrosis, cancer, and cardiovascular disorders, where collagen dysregulation is prevalent. Research into P4HTM focuses on understanding its enzymatic mechanisms, substrate specificity, and regulatory pathways that control its activity. Furthermore, there is growing interest in its potential as a therapeutic target, as inhibiting or enhancing P4HTM activity could offer novel strategies for treating collagen-related diseases. The investigation of P4HTM not only provides insights into fundamental biological processes but also highlights the intricate relationship between protein modifications and disease pathogenesis, paving the way for innovative biomedical applications and drug development aimed at modulating collagen dynamics in pathological conditions.
