Analytical Data
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Gene name
RAB33B
- Application
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Alternative Names
RAB33B；Ras-related Protein Rab-33B
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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
Q9H082
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Expression Region
1-229aa
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AA Sequence
MAEEMESSLEASFSSSGAVSGASGFLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVEIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPSWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQPPDNGIILKPEPKPAMTCWC
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Molecular Weight
31.8 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
RAB33B is a member of the RAB family of small GTPases, which play crucial roles in regulating intracellular vesicular transport and membrane trafficking. Research into RAB33B has gained momentum due to its involvement in various cellular processes, including autophagy, secretion, and organelle dynamics. Recent studies have indicated that RAB33B may participate in the modulation of autophagic pathways, impacting cellular homeostasis and potential implications in diseases such as cancer and neurodegeneration. Additionally, RAB33B has been observed to interact with specific effector proteins that facilitate its role in endosomal transport and lysosomal biogenesis. The reconstitution of RAB33B as a recombinant protein is vital for elucidating its functional mechanisms and interactions within the cellular context. This approach allows for detailed biochemical analyses and structural studies, paving the way for understanding how RAB33B regulates vesicle trafficking pathways. Furthermore, given the growing interest in the therapeutic potential of targeting RAB proteins, particularly in the context of disease mechanisms, the characterization of RAB33B could unveil novel strategies for treatment and intervention. Thus, the study of RAB33B recombinant protein holds promise for advancing our understanding of intracellular dynamics and exploring its role in health and disease.
