Recombinant Human ADSS 293 Cell Lysate
Cat.No. : | ADSS-8994HCL |
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Description : | Antigen standard for adenylosuccinate synthase (ADSS) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection. |
Source : | HEK 293 cells |
Species : | Human |
Components : | This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol). |
Size : | 0.1 mg |
Storage Instruction : | Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored at -20°C. Product is guaranteed 6 months from the date of shipment. |
Applications : | ELISA, WB, IP. WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane. |
Gene Name : | ADSS adenylosuccinate synthase [ Homo sapiens ] |
Official Symbol : | ADSS |
Synonyms : | ADEH; ADSS 2 |
Gene ID : | 159 |
mRNA Refseq : | NM_001126.3 |
Protein Refseq : | NP_001117.2 |
MIM : | 103060 |
UniProt ID : | P30520 |
Chromosome Location : | 1q44 |
Pathway : | Adenine ribonucleotide biosynthesis, IMP => ADP,ATP, organism-specific biosystem;Adenine ribonucleotide biosynthesis, IMP => ADP,ATP, conserved biosystem;Alanine, aspartate and glutamate metabolism, organism-specific biosystem;Alanine, aspartate and glutamate metabolism, conserved biosystem;Metabolism, organism-specific biosystem; |
Function : | GTP binding;adenylosuccinate synthase activity;adenylosuccinate synthase activity;magnesium ion binding;phosphate ion binding; |
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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 expression of Adss protein is regulated at both the transcriptional and post-transcriptional levels by various factors, such as transcription factors and microRNAs.
Adss protein is primarily involved in the biosynthesis of purine nucleotides and participates in the de novo purine synthesis pathway.
Adss protein can potentially form protein complexes or interact with other proteins, which may have functional implications in cellular processes related to purine metabolism.
Currently, there are no specific pharmacological agents targeting Adss protein. However, further understanding of its regulation and functional implications may lead to the development of potential therapeutic approaches for related conditions.
Experimental techniques such as enzymatic assays and substrate analysis have been used to study the enzymatic activity of Adss protein.
Dysregulation or dysfunction of Adss protein can disrupt purine metabolism, potentially contributing to disorders involving abnormalities in nucleotide synthesis.
Genetic variations or mutations in the Adss gene may impact the function or stability of Adss protein, potentially leading to disorders associated with purine metabolism.
Adss protein activity may be regulated or influenced by cellular factors and cofactors, including ATP and magnesium ions.
The subcellular localization of Adss protein is predominantly cytoplasmic, but it may undergo changes under specific cellular conditions or stimuli.
The structural features of Adss protein, including conserved domains and active sites, contribute to its enzymatic activity and substrate specificity in purine biosynthesis.
Customer Reviews (3)
Write a reviewUnderstanding protein-protein interaction networks in mitochondrial function.
Detecting protein-protein interactions in extracellular matrix assembly.
Exploring protein-protein interactions involved in stem cell differentiation.
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