Analytical Data
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Gene name
PGAM5
- Application
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Biological Activity
Human PGAM5 immobilized on CM5 Chip can bind LFHP-1c with an affinity constant of 425.8 nM as determined in a SPR assay. Human PGAM5 immobilized on CM5 Chip can bind LFHP-1c with an affinity constant of 425.8 nM as determined in a SPR assay.
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Alternative Names
Bcl-XL-binding protein v68; Phosphoglycerate mutase family member 5
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q96HS1-1
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Expression Region
K30-S289
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Protein Length
Partial
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Molecular Weight
31-40 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
PGAM5 (Phosphoglycerate Mutase 5) is a member of the phosphoglycerate mutase family, implicated in various cellular processes, including metabolism and signaling. Research interest in PGAM5 has surged due to its pivotal role in regulating mitochondrial dynamics and apoptosis. It functions as a key player in the regulation of cell fate decisions, responding to cellular stress and helping maintain mitochondrial integrity. Dysregulation of PGAM5 has been linked to several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. The recombinant protein form of PGAM5 offers a valuable tool for dissecting its functional mechanisms and interactions within cellular pathways. Additionally, the production of PGAM5 as a recombinant protein allows for detailed biochemical studies, including enzyme kinetics and structure-function analyses. Understanding PGAM5’s role at the molecular level is vital for developing targeted therapeutic strategies. As researchers strive to uncover the complexities of PGAM5's involvement in cellular processes, the recombinant protein serves as a crucial asset in elucidating its contributions to health and disease. This research opens avenues for potential interventions in various pathologies associated with mitochondrial dysfunction and highlights the importance of PGAM5 in cellular homeostasis.
