Analytical Data
-
Gene name
DYNLRB1
- Application
-
Alternative Names
Bithoraxoid-like protein ;BLPDynein light chain 2A, Cytoplasmic domainDynein-associated protein Km23Roadblock domain-containing protein 1
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NP97
-
Expression Region
3-96aa
-
Molecular Weight
26.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DYNLRB1 (Dynamin-like protein DYNLRB1) is a member of the dynamin superfamily, primarily known for its role in intracellular transport and actin dynamics. The protein plays a crucial role in cell motility, endocytic trafficking, and organelle dynamics. With the increasing interest in understanding the molecular mechanisms underlying cellular processes, DYNLRB1 has emerged as a significant focus due to its involvement in various physiological and pathological conditions, including neurodegenerative diseases and cancers. Recent studies have highlighted its capacity to interact with a range of cellular partners, suggesting that it may act as a regulatory hub for intracellular signaling pathways. To investigate the functional properties of DYNLRB1, researchers have been developing recombinant protein systems which allow for in-depth analysis of its structure, dynamics, and interaction with other cellular components. These studies aim to elucidate the specific roles DYNLRB1 plays in cellular processes and its potential as a therapeutic target. Understanding the protein's functions and interactions at a molecular level not only enhances our comprehension of basic cell biology but also paves the way for novel approaches in treating diseases linked to dysregulated cellular transport and dynamics. Overall, the research on DYNLRB1 recombinant proteins is crucial for uncovering the intricate roles this protein plays in the cellular environment, ultimately contributing to advancements in biomedical research and therapeutic interventions.
