Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P02768 |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modification, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO-carrier. |
molecular weight | The protein has a predicted MW of 69.4 kDa. Due to glycosylation, the protein migrates to 69-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human Serum Albumin Protein 4223
$38.00 – $125.00
Summary
- Expression: HEK293
- Binding assay: Yes (SPR)
- Amino Acid Range: Asp25-Leu609
Human Serum Albumin Protein 4223
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modification, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO-carrier. |
Protein names Albumin |
Gene names ALB,ALB GIG20 GIG42 PRO0903 PRO1708 PRO2044 PRO2619 PRO2675 UNQ696/PRO1341 |
Protein family ALB/AFP/VDB family |
Mass 9606Da |
Function Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017). |
Subellular location Secreted. |
Tissues Plasma. |
Structure Interacts with FCGRT; this interaction regulates ALB homeostasis (PubMed:28330995). Interacts with TASOR (By similarity). In plasma, occurs in a covalently-linked complex with chromophore-bound alpha-1-microglobulin with molar ratio 1:2 and 1:1; this interaction does not prevent fatty acid binding to ALB. |
Post-translational modification Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.; Glycated in diabetic patients.; Phosphorylated by FAM20C in the extracellular medium.; Acetylated on Lys-223 by acetylsalicylic acid. |
Target Relevance information above includes information from UniProt accession: P02768 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
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Protocols
relevant to this product |
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Documents
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