Analytical Data
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Gene name
RILPL2
- Application
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Alternative Names
FLJ30380; FLJ32372; MGC7036; p40phox-binding protein; Rab-interacting lysosomal protein-like 2; RILP-like protein 2; RILPL2; RIPL2_HUMAN; RLP2
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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
Q969X0
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Expression Region
1-211 aa
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AA Sequence
MEEPPVREEE EEEGEEDEER DEVGPEGALG KSPFQLTAED VYDISYLLGR ELMALGSDPR VTQLQFKVVR VLEMLEALVN EGSLALEELK MERDHLRKEV EGLRRQSPPA SGEVNLGPNK MVVDLTDPNR PRFTLQELRD VLQERNKLKS QLLVVQEELQ CYKSGLIPPR EGPGGRREKD AVVTSAKNAG RNKEEKTIIK KLFFFRSGKQ T
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Molecular Weight
23.9 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
RILPL2, or RILP-like protein 2, is a member of the RILP family known for its involvement in intracellular transport and membrane trafficking processes. Research into RILPL2 has gained significance due to its potential role in various cellular functions and its implication in several diseases, including neurodegeneration and cancer. The protein is characterized by the presence of a coiled-coil domain, which is essential for its interactions with other cellular proteins involved in the endosomal-lysosomal pathway. This pathway is crucial for the degradation and recycling of cellular components, influencing cellular homeostasis. Elevated or altered expression of RILPL2 has been associated with pathological conditions, highlighting the need to understand its biological functions and regulatory mechanisms. Recent studies have focused on the potential of RILPL2 as a target for therapeutic intervention, making it a topic of considerable interest within the fields of cell biology and molecular medicine. To further elucidate the protein's functions, researchers have developed recombinant RILPL2 constructs, enabling detailed studies on its interactions, localization, and biological roles in various cellular contexts. Understanding RILPL2's functions at a molecular level could provide insights into its contribution to disease mechanisms and pave the way for innovative therapeutic strategies.
