Analytical Data
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Gene name
DPH2
- Application
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Alternative Names
DPH2；DPH2L2;2-(3-amino-3-carboxypropyl)histidine synthase subunit 2
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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
Q9BQC3
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Expression Region
1-489aa
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AA Sequence
MESMFSSPAEAALQRETGVPGLLTPLPDLDGVYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACLSPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALEALATLLRPRYLDLLVSSPAFPQPVGSLSPEPMPLERFGRRFPLAPGRRLEEYGAFYVGGSKASPDPDLDPDLSRLLLGWAPGQPFSSCCPDTGKTQDEGARAGRLRARRRYLVERARDARVVGLLAGTLGVAQHREALAHLRNLTQAAGKRSYVLALGRPTPAKLANFPEVDVFVLLACPLGALAPQLSGSFFQPILAPCELEAACNPAWPPPGLAPHLTHYADLLPGSPFHVALPPPESELWETPDVSLITGDLRPPPAWKSSNDHGSLALTPRPQLELAESSPAASFLSSRSWQGLEPRLGQTPVTEAVSGRRGIAIAYEDEGSG
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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
DPH2 (Diphosphate-Dependent Heme Synthase 2) is a key enzyme involved in the biosynthetic pathway of heme, a vital prosthetic group for many hemoproteins essential for various biological processes. Research into DPH2 has gained momentum due to its role in heme synthesis and its potential implications in health and disease. Mutations or dysregulation of heme biosynthesis can lead to a range of disorders, including anemia and neurological diseases. Understanding the function and regulation of DPH2 is crucial for elucidating these pathways and developing therapeutic strategies. Recent studies have focused on the recombinant production of DPH2 protein, allowing researchers to investigate its enzymatic properties, substrate specificity, and interaction with other proteins in the heme biosynthetic pathway. By producing DPH2 in a heterologous system, scientists can explore its structure-function relationships and the effects of specific mutations, which may further our understanding of its physiological roles and potential involvement in pathologies. The comprehensive characterization of DPH2 at both molecular and biochemical levels could pave the way for innovative therapeutic approaches targeting heme-related disorders, highlighting the importance of this enzyme in cellular metabolism and its potential as a therapeutic target.
