Recombinant Rat Arl1, His-tagged
Cat.No. : | Arl1-3211R |
Product Overview : | ADP-ribosylation factor-like protein 1 (Arl1) |
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Description : | regulates the structure and function of the Golgi apparatus . |
Source : | E. Coli or Yeast |
Species : | Rat |
Tag : | His |
Form : | This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications. |
Protein length : | 181 |
Purity : | >90% |
Notes : | Small volumes of Arl1 recombinant protein may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice. |
Storage : | Store at -20 degree C. For extended storage, store at -20 or -80 degree C. |
Storage Buffer : | PBS pH 7.4, 50% glycerol |
Warning : | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Gene Name : | Arl1 ADP-ribosylation factor-like 1 [ Rattus norvegicus ] |
Official Symbol : | Arl1 |
Synonyms : | ARL1; ADP-ribosylation factor-like 1; ADP-ribosylation factor-like protein 1; MGC72836; |
Gene ID : | 64187 |
mRNA Refseq : | NM_022385 |
Protein Refseq : | NP_071780 |
Function : | GTP binding; GTP binding; GTP binding; GTPase activity; GTPase activity; enzyme activator activity; enzyme activator activity; metal ion binding; nucleotide binding; protein domain specific binding; |
Products Types
◆ Recombinant Protein | ||
ARL1-714M | Recombinant Mouse ARL1 Protein, His (Fc)-Avi-tagged | +Inquiry |
Arl1-256M | Recombinant Mouse Arl1 Protein, MYC/DDK-tagged | +Inquiry |
ARL1-432R | Recombinant Rat ARL1 Protein, His (Fc)-Avi-tagged | +Inquiry |
ARL1-801H | Recombinant Human ARL1 protein, GST-tagged | +Inquiry |
ARL1-9847H | Recombinant Human ARL1, His-tagged | +Inquiry |
◆ Lysates | ||
ARL1-8724HCL | Recombinant Human ARL1 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (16)
Ask a questionYes, ARL1 can undergo post-translational modifications such as lipidation with myristate or palmitate groups. These modifications aid in membrane association and regulate the localization and function of ARL1 in vesicular trafficking.
Currently, there are no known genetic disorders directly associated with ARL1 mutations. However, dysregulation of vesicular trafficking processes, for which ARL1 is essential, can contribute to pathological conditions. Further research may uncover potential links between ARL1 dysfunction and specific genetic disorders.
While the primary role of ARL1 is in vesicular trafficking, recent studies have suggested additional functions for ARL1 in autophagy, cilia formation, and cytoskeleton organization. These emerging roles expand the potential impact of ARL1 in maintaining cellular homeostasis.
While there is no direct association between ARL1 mutations and specific diseases, dysregulation of ARL1-mediated vesicular trafficking processes can contribute to pathological conditions. For example, defects in Golgi-ER trafficking and autophagy have been linked to neurodegenerative diseases and cancer, suggesting potential roles for ARL1 dysfunction in these disorders.
ARL1 is expressed in a wide range of cell types and tissues, suggesting its ubiquitous presence in most cellular systems. However, its expression levels may vary depending on the specific cell type and the physiological state of the cell.
ARL1 itself is not extensively involved in signaling pathways. However, its interactions with effector proteins indirectly contribute to the regulation of various signaling cascades, such as the Wnt signaling pathway and the MAPK/ERK pathway, which are crucial for cell growth, development, and differentiation.
Currently, no specific human diseases have been directly linked to ARL1 dysfunction. However, alterations in vesicular trafficking processes, for which ARL1 is essential, can contribute to various pathological conditions such as neurodegenerative disorders and certain cancers.
Currently, there are no specific drugs or compounds developed to directly modulate ARL1 activity. However, as our understanding of ARL1 function advances, it may provide insights into potential targets for therapeutic intervention in diseases related to vesicular trafficking defects.
ARL1 is primarily localized to the Golgi apparatus and the ER, where it regulates vesicular trafficking events between these organelles. However, studies have also reported a partial distribution of ARL1 in other cellular compartments, including the plasma membrane and the trans-Golgi network, suggesting its involvement in diverse membrane trafficking pathways.
ARL1 shares similarities with other small GTPases, such as the ADP-ribosylation factor (ARF) proteins. While ARL1 and ARF proteins belong to the same GTPase superfamily, they have distinct functions and interactions with specific effector proteins. However, cross-talk between ARL1 and ARF proteins may occur in some cellular contexts, regulating membrane trafficking processes.
ARL1 regulates the recruitment and actions of effector proteins involved in vesicle tethering, fusion, and cargo sorting between the Golgi apparatus and ER. By facilitating these processes, ARL1 ensures efficient and accurate transport of proteins and lipids, maintaining the overall integrity and function of the endomembrane system within the cell.
Yes, ARL1 interacts with various effector proteins involved in vesicular trafficking, such as GRIP domain-containing ARF-binding protein 2 (GGA2), golgin subfamily A member 1 (GOLGA1), and golgin subfamily B member 1 (GOLGB1). These interactions facilitate the targeting and fusion of vesicles at specific cellular compartments.
Depletion or knockout of ARL1 in cells has been reported to cause disrupted Golgi-ER trafficking, altered lysosome morphology, impaired autophagy, and defects in cilia formation. These consequences highlight the critical role of ARL1 in maintaining organelle dynamics and cellular processes.
Current research on ARL1 focuses on elucidating its precise molecular mechanisms and identifying additional binding partners and effector proteins. Additionally, studies are exploring the functional implications of ARL1 in diseases with vesicular trafficking defects, which may offer new therapeutic strategies.
Currently, no specific therapeutics have been developed to directly target ARL1. However, understanding its role in vesicular trafficking may provide insights into potential therapeutic strategies for diseases associated with dysregulated vesicular transport processes.
ARL1 protein is activated by the exchange of GDP (guanosine diphosphate) for GTP (guanosine triphosphate) through the action of guanine nucleotide exchange factors (GEFs). Once activated, ARL1 interacts with effector proteins to carry out its cellular functions.
Customer Reviews (8)
Write a reviewThe ARL1 protein is renowned for its exceptional quality, making it a perfect match for my experimental requirements.
Researchers have successfully utilized ARL1 protein in electron microscopy studies, unraveling crucial insights into protein interactions and conformational changes.
This can involve organizing conferences, workshops, and webinars to discuss the latest advancements, share research findings, and broaden the understanding of ARL1 function
the ARL1 protein exhibits superior performance across a range of experimental applications.
In addition to its high-quality attributes, the manufacturer of the ARL1 protein offers exemplary technical support.
The exceptional performance of ARL1 protein in both ELISA and protein electron microscopy structure analysis positions it as a valuable tool in a broad range of research applications.
This technical support is invaluable, especially for researchers who may be new to working with ARL1 protein or if they encounter specific difficulties while conducting their experiments.
Its versatility allows for its successful implementation in diverse areas such as molecular biology, cellular assays, and protein-protein interactions.
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