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Key Documents

A0433

Sigma-Aldrich

Anti-Albumin antibody produced in rabbit

IgG fraction of antiserum

Synonyme(s) :

Anti Albumin Antibody

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Poids mol.

antigen 65 kDa

Espèces réactives

human

Technique(s)

indirect ELISA: 1:25,000
quantitative precipitin assay: 4.0-6.0 mg/mL

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ALB(213)

Description générale

Albumin is the most abundant plasma protein in humans.
Albumin, the major protein produced by liver cells, represents more than half of the total protein content of human serum. Many other body fluids also contain albumin.

Spécificité

Rabbit polyclonal anti-Albumin antibody reacts with human serum and human albumin.

Immunogène

purified human albumin

Application

Anti-Albumin antibody produced in rabbit has been used in:
  • immunocytochemistry
  • immunoassay of amino-terminal fragments(ATF)-human serum albumin (HSA)
  • canstatin (Can) - human serum albumin (HSA)
  • enzyme-linked immunosorbent assay (ELISA)

Actions biochimiques/physiologiques

Three major functions for serum albumin have been proposed: maintenance of osmotic pressure, transportation of a variety of substances and an endogenous source of amino acids. The primary sites of albumin degradation are not known, but the protein can be metabolized by almost every organ in the body. Determination of serum albumin levels is a widely used screening test in clinical medicine. A decrease in serum albumin levels may indicate disease states such as malnutrition, cirrhosis, nephrotic syndrome, diabetes, gastrointestinal and hepatic diseases, thermal burns and pulmonary disease. High levels of albumin are associated with dehydration. Albumin turnover is seen in infants with iron deficiency anemia. Advanced liver disease is associated with oxidative damage of albumin.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.2, containing 15 mM sodium azide

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Shahid S Siddiqui et al.
American journal of physiology. Lung cellular and molecular physiology, 286(5), L1016-L1026 (2004-01-20)
Vascular endothelial cells undergo albumin endocytosis using a set of albumin binding proteins. This process is important for maintaining cellular homeostasis. We showed by several criteria that the previously described 73-kDa endothelial cell surface albumin binding protein is the 75-kDa
Activin a efficiently specifies definitive endoderm from human embryonic stem cells only when phosphatidylinositol 3-kinase signaling is suppressed
McLean AB, et al.
Stem Cells, 25(1), 29-38 (2007)
F Apparailly et al.
Gene therapy, 9(3), 192-200 (2002-02-23)
Plasmin is essential for metalloproteases activation, endothelial cell migration and degradation of the extracellular matrix. The process is common to neoangiogenesis pannus formation and cartilage degradation within arthritic joints. Since 80% of synovial cells express urokinase plasminogen activator receptor (uPAR)
Canstatin gene electrotransfer combined with radiotherapy: preclinical trials for cancer treatment
Magnon C, et al.
Gene Therapy, 15(21), 1436-1436 (2008)
A gene transfer comparative study of HSA-conjugated antiangiogenic factors in a transgenic mouse model of metastatic ocular cancer
Frau E, et al.
Cancer Gene Therapy, 14(3), 251-251 (2007)

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