Analytical Data
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Gene name
FARP2
- Application
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Alternative Names
FERM domain-including RhoGEF;FIR;FERM. RhoGEF and pleckstrin domain-containing protein 2;Pleckstrin homology domain-containing family C member 3;PH domain-containing family C member 3
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O94887
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Expression Region
44-324aa
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AA Sequence
LHLRVKLLDNTMEIFDIEPKCDGQVLLTQVWKRLNLVECDYFGMEFQNTQSYWIWLEPMKPIIRQIRRPKNVVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCADTTAALLTSHLLQSEIGDYDETLDREHLKVNEYLPGQQHCLEKILEFHQKHVGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKIQLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLLD
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Molecular Weight
40.3 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
FARP2 (FERM, ARHGEF, and Pleckstrin domain-containing protein 2) is a member of the FARP family of proteins that plays a crucial role in cellular signaling and is implicated in various physiological processes. Originally identified for its involvement in the regulation of small GTPases, particularly Rho and Rac, FARP2 is known to influence cytoskeletal dynamics, cell polarization, and motility. Research has increasingly focused on FARP2 due to its potential implications in pathological conditions, such as cancer progression and neurodevelopmental disorders. The protein's structure, featuring FERM and pleckstrin homology (PH) domains, suggests it plays multifaceted roles in membrane interactions and signal transduction pathways. Studies aiming to produce recombinant FARP2 protein have gained traction as they enable detailed investigations into its biochemical properties, interaction networks, and functional mechanisms. Furthermore, understanding FARP2's role in cell signaling can uncover novel therapeutic targets, potentially leading to advances in treatments for diseases associated with FARP2 dysregulation.
