Recombinant Human C6orf105 293 Cell Lysate
Cat.No. : | ADTRP-8004HCL |
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Description : | Antigen standard for chromosome 6 open reading frame 105 (C6orf105), transcript variant 2 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 : | ADTRP androgen-dependent TFPI-regulating protein [ Homo sapiens ] |
Official Symbol : | ADTRP |
Synonyms : | AIG1L; C6orf105; dJ413H6.1; androgen-dependent TFPI-regulating protein; androgen-dependent TPF1-regulating protein |
Gene ID : | 84830 |
mRNA Refseq : | NM_001143948 |
Protein Refseq : | NP_001137420 |
MIM : | 614348 |
UniProt ID : | Q96IZ2 |
Chromosome Location : | 6p24.1 |
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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 questionPost-translational modifications, such as phosphorylation or ubiquitination, and regulatory factors like lipid signals or protein-protein interactions, may modulate the activity or stability of ADTRP protein.
Experimental techniques such as knockout or overexpression studies, as well as cellular and molecular biology approaches, have been employed to investigate the functional significance of ADTRP protein in lipid metabolism and cellular processes.
ADTRP protein exhibits tissue-specific expression, with higher levels observed in the heart, skeletal muscle, and adipose tissue. Factors involved in its regulation include transcriptional control and tissue-specific signaling pathways.
The subcellular localization of ADTRP protein is determined by specific targeting sequences and mechanisms that facilitate its transport and integration into the endoplasmic reticulum membrane.
ADTRP protein contains specific structural features, including transmembrane domains and potential lipid-binding motifs, that are critical for its function and interaction with lipid molecules or membrane components.
The enzymatic activity of ADTRP protein, potentially involved in lipid metabolism, can be measured or quantified using enzymatic assays that assess substrate utilization or product formation.
Genetic variations or mutations in the ADTRP gene may impact the expression or function of ADTRP protein, potentially contributing to lipid metabolism disorders or cardiovascular diseases.
ADTRP protein is implicated in lipid metabolism and membrane biology, potentially playing a role in lipid droplet formation, lipid storage, or lipid transport processes.
ADTRP protein has been shown to interact with other proteins, such as enzymes involved in lipid metabolism or membrane trafficking, suggesting potential roles in lipid homeostasis and intracellular transport processes.
Dysregulation or dysfunction of ADTRP protein may affect cellular lipid homeostasis, leading to imbalances in lipid metabolism and potential contributions to diseases such as obesity or cardiomyopathies.
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Write a reviewDetermining protein-protein interaction interfaces using peptide array assays.
Characterizing protein-protein interactions involved in cell migration.
Exploring protein-protein interactions involved in angiogenesis pathways.
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