Recombinant Mouse ADSSL1 Protein Pre-coupled Magnetic Beads
Cat.No. : | ADSSL1-370M-B |
Product Overview : | The Recombnant protein was conjugated to magnetic beads. This ready-to-use, pre-coupled magnetic beads are in uniform particle size and narrow size distribution with large surface area, which is conducive to convenient and fast capture target molecules with high specificity and achieve magnetic separation. This product can be equipped with automation equipment for high-throughput operations. |
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Source : | HEK293 |
Species : | Mouse |
Form : | Solution |
Particle size : | ~2 μm |
Beads Surface : | Hydrophilic |
Capacity : | > 200 pmol rabbit IgG/ mg beads |
Applications : | Immunoassay, In vitro diagnostics, cell sorting, Immunoprecipitation/Co-precipitation, Protein/antibody separation and purification. |
Stability : | Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions. |
Storage : | 2-8℃. Do not to freeze thaw the Beads |
Concentration : | 10mg beads/mL |
Storage Buffer : | PBS buffer |
Gene Name : | Adssl1 adenylosuccinate synthetase like 1 [ Mus musculus ] |
Official Symbol : | ADSSL1 |
Gene ID : | 11565 |
mRNA Refseq : | NM_007421.2 |
Protein Refseq : | NP_031447.1 |
UniProt ID : | P28650 |
Products Types
◆ Recombinant Protein | ||
ADSSL1-370M | Recombinant Mouse ADSSL1 Protein, His (Fc)-Avi-tagged | +Inquiry |
Adssl1-550M | Recombinant Mouse Adssl1 Protein, MYC/DDK-tagged | +Inquiry |
Adssl1-3189M | Recombinant Mouse Adssl1, His-tagged | +Inquiry |
ADSSL1-3188B | Recombinant Bovine ADSSL1, His-tagged | +Inquiry |
ADSSL1-1392M | Recombinant Mouse ADSSL1 Protein | +Inquiry |
◆ Lysates | ||
ADSSL1-8993HCL | Recombinant Human ADSSL1 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 (10)
Ask a questionThe subcellular localization of ADSSL1 protein is primarily within mitochondria, facilitated by mitochondrial targeting sequences and import machinery.
Post-translational modifications, such as phosphorylation or acetylation, and regulatory factors like metabolic signals or protein-protein interactions, may modulate the activity or stability of ADSSL1 protein.
ADSSL1 protein can interact with other enzymes involved in purine metabolism, forming complexes that regulate nucleotide synthesis and energy metabolism.
Genetic variations or mutations in the ADSSL1 gene can impact the expression or function of ADSSL1 protein, potentially leading to disorders associated with purine metabolism abnormalities.
ADSSL1 protein plays a critical role in purine nucleotide metabolism, contributing to the deamination and recycling of adenylosuccinate to maintain nucleotide homeostasis.
ADSSL1 protein contains conserved structural domains, including a catalytic domain and nucleotide-binding motifs, that contribute to its enzymatic activity and substrate specificity.
The enzymatic activity of ADSSL1 protein, catalyzing the conversion of adenylosuccinate to AMP, can be measured using enzymatic assays that quantify substrate utilization and product formation.
Experimental approaches such as knockout or overexpression studies have been utilized to investigate the functional significance of ADSSL1 protein, revealing its role in cellular metabolism and energy balance.
ADSSL1 protein exhibits tissue-specific expression, with higher levels observed in skeletal muscle, heart, and brain. Factors involved in its regulation include transcriptional control and signaling pathways.
Dysregulation or dysfunction of ADSSL1 protein can disrupt cellular purine metabolism, leading to imbalances in nucleotide levels and potential contributions to diseases such as neurodegenerative disorders or metabolic syndromes.
Customer Reviews (3)
Write a reviewExploring protein-protein interactions involved in intracellular trafficking.
Detecting protein-protein interactions in membrane receptor signaling.
Understanding protein-protein interaction networks in DNA repair processes.
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