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Key Documents

A8301

Sigma-Aldrich

Albumin, glycated human

lyophilized powder

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

biological source

human

Quality Level

assay

90-100% protein basis (biuret)

form

lyophilized powder

extent of labeling

1-5 mol hexose (as fructosamine) per mol albumin

technique(s)

cell culture | mammalian: suitable

UniProt accession no.

storage temp.

−20°C

InChI

1S/C3F8/c4-1(5,2(6,7)8)3(9,10)11

InChI key

QYSGYZVSCZSLHT-UHFFFAOYSA-N

Gene Information

human ... ALB(213)

General description

Albumin gene is mapped to human chromosome 4q13.3. It is synthesized as a preproalbumin with 609 amino acids in the liver. The mature albumin comprising 585 residues, is generated by the cleavage of signal peptide. Albumin is the major circulating protein in serum. It comprises three domains (I, II and III), each of which is subdivided into two subdomains A and B. A total of six ligand binding site is associated with albumin. Domain IIA and IIIA harbor small heterocyclic or aromatic compounds binding site. Long-chain fatty acid binding sites is present in IB and IIIB domains.

Application

Albumin, glycated human has been used:
  • as a component of serum-free medium for retinal microglia activation
  • to stimulate immortalised proximal tubule epithelial (HK-2) cells for fibronectin production
  • as medium supplement in human retinal microvascular endothelial cells (HRMECs) cultures to test its effect on family with sequence similarity 18, member B (FAM18B) expression


Naturally occurring glycated albumin is a sensitive indicator of glycemic control by diabetic patients.

Biochem/physiol Actions

Albumin is crucial for physiological processes and is the major transporter for lipids, metal ions and amino acids. It has antioxidant functionality and binds to drugs as well. Mutation in the albumin gene is implicated in an autosomal recessive disorder called Analbuminemia, which is characterized by low levels of albumin. The major glycation site is lysine 525 in albumin. Glycated albumin is a marker of glycemia in diabetes mellitus patients and is useful in assessment of HbA1c based glycemic control.

Physical form

Lyophilized powder containing citrate buffer salts

Preparation Note

Glycated in vitro

Other Notes

View more information on human serum albumin.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

CCL18 synergises with high concentrations of glucose in stimulating fibronectin production in human renal tubuloepithelial cells
Montero RM, et al.
BMC Nephrology, 17(1), 139-139 (2016)
Glycated albumin is a better glycemic indicator than glycated hemoglobin values in hemodialysis patients with diabetes: effect of anemia and erythropoietin injection
Inaba M, et al.
Journal of the American Society of Nephrology, 18(3), 896-903 (2007)
Glycated albumin: a potential biomarker in diabetes
Freitas P, et al.
Archives of endocrinology and metabolism, 61(3), 296-304 (2017)
A novel mutation in the albumin gene (c. 1A> C) resulting in analbuminemia
Caridi G, et al.
European Journal of Clinical Investigation, 43(1), 72-78 (2013)
Mizuho Nakayama et al.
Nature communications, 11(1), 2333-2333 (2020-05-13)
Missense-type mutant p53 plays a tumor-promoting role through gain-of-function (GOF) mechanism. In addition, the loss of wild-type TP53 through loss of heterozygosity (LOH) is widely found in cancer cells. However, malignant progression induced by cooperation of TP53 GOF mutation and

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