Analytical Data
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Gene name
LMW-PTP/ACP1
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简介
LMW-PTP/ACP1, a phosphatase, acts on tyrosine phosphorylated proteins, low-molecular-weight aryl phosphates, and natural and synthetic acyl phosphates. Notably, there are substrate specificity differences between isoform 1 and isoform 2, with isoform 2 lacking phosphatase activity. LMW-PTP/ACP1 Protein, Human (C-His) is the recombinant human-derived LMW-PTP/ACP1 protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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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
P24666-2
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Expression Region
A2-H158
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Protein Length
Full Length of Isoform-2 Mature Protein
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Molecular Weight
18.0 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
LMW-PTP (Low Molecular Weight Protein Tyrosine Phosphatase) and ACP1 (Acidic Calmodulin-Binding Protein-1) are pivotal enzymes in cell signaling pathways, playing crucial roles in regulating cellular responses through the dephosphorylation of tyrosine residues on proteins. The study of these proteins is particularly important due to their involvement in various physiological processes, including cell growth, differentiation, and metabolism, as well as their potential link to diseases such as cancer and diabetes. LMW-PTP, being a member of the protein tyrosine phosphatase family, has been implicated in oxidative stress responses and has shown interactions with oncogenes and tumor suppressors, suggesting its relevance in cancer biology. On the other hand, ACP1 is known for its role in signal transduction and calcium signaling pathways, influencing processes such as neuronal function and immune response. The generation of recombinant proteins for LMW-PTP and ACP1 allows for detailed biochemical and structural studies, enabling researchers to unravel their mechanisms of action, investigate their functions in various cellular contexts, and explore their potential as therapeutic targets. By utilizing recombinant DNA technology, these proteins can be produced in a controlled manner, providing a platform for high-throughput screening and compound identification that could lead to novel treatment strategies. Understanding the intricacies of LMW-PTP and ACP1 through recombinant protein studies not only deepens our comprehension of cell signaling mechanisms but also opens avenues for developing new interventions in diseases where these pathways are dysregulated.
