Analytical Data
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Gene name
PTPLB
- Application
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Alternative Names
PTPLB；PTPLB；Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 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
Q6Y1H2
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Expression Region
2-254aa
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AA Sequence
AAVAATAAAKGNGGGGGRAGAGDASGTRKKKGPGPLATAYLVIYNVVMTAGWLVIAVGLV RAYLAKGSYHSLYYSIEKPLKFFQTGALLEILHCAIGIVPSSVVLTSFQVMSRVFLIWAV THSVKEVQSEDSVLLFVIAWTITEIIRYSFYTFSLLNHLPYLIKWARYTLFIVLYPMGVS GELLTIYAALPFVRQAGLYSISLPNKYNFSFDYYAFLILIMISYIPIFPQLYFHMIHQRR KILSHTEEHKKFE
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Molecular Weight
28.3 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
The research on the PTPLB (Protein Tyrosine Phosphatase-Like B) restructured protein emerges from the growing interest in understanding the role of protein tyrosine phosphatases (PTPs) in cellular signaling and regulation. PTPs are crucial enzymes that remove phosphate groups from tyrosine residues on proteins, thereby influencing various biological processes such as cell growth, differentiation, and metabolism. Dysregulation of PTP activity has been implicated in several diseases, including cancer and diabetes. PTPLB, specifically, is a member of the PTP family that has garnered attention for its potential involvement in modulating immune responses and neurodegenerative diseases. Recent studies suggest that manipulating PTPLB activity could offer novel therapeutic avenues for conditions characterized by hyperactive or dysregulated signaling pathways. By restructuring PTPLB through techniques such as gene editing and protein engineering, researchers aim to enhance our understanding of its functional mechanisms and explore its potential as a target for drug discovery. This research not only deepens the comprehension of PTP roles in health and disease but also paves the way for innovative therapeutic strategies that leverage the precise modulation of phosphatase activities in various pathological contexts.
