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A3293

Sigma-Aldrich

Anti-Human Albumin antibody produced in rabbit

whole antiserum

Synonyme(s) :

Albumin Antibody, Albumin Antibody - Anti-Human Albumin antibody produced in rabbit, Anti Human 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

whole antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Poids mol.

antigen 66.437-66.6 kDa

Contient

15 mM sodium azide

Espèces réactives

human

Technique(s)

indirect ELISA: 1:60,000
quantitative precipitin assay: 2.4-3.6

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′s primary structure is composed of a single chain of amino acids and the secondary structure is composed of α-helix of six turns and 17 disulfide bridges. The tertiary structure is 3D and is composed of three domains I II and III. Each of these domains are made of sub-domains IAB, IC, IIAB, IIC, IIIAB, IIIC, respectively.

Spécificité

Anti-human albumin antibodies are specific for human albumin.

Immunogène

Human albumin

Application

Anti-Human Albumin antibody has been used in enzyme linked immunosorbent assay (ELISA) and in immobilization of antibodies for human serum albumin (HSA).
Anti-human albumin antibody may be used in quantitative precipitin assay, high-throughput protein microarray analysis and immunocytochemistry .
Rat hepatocytes were grown on collagen-coated coverslips, fixed in formalin and permeablized with methanol prior to incubation with rabbit anti-human albumin antibody.

Actions biochimiques/physiologiques

Albumin is a transport protein that binds a broad range of ligands such as fatty acids, bilirubin, hemin, drugs, amino acids and ions among several others . Albumin may also function as a zinc carrier protein and consequently regulate physiological processes .
Albumin plays a major role in transportation and deposition of many exogenous and endogenous substances in blood.

Forme physique

Supplied as a liquid containing 15mM sodium azide as preservative.

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Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Sreedevi Karthi et al.
Experimental and therapeutic medicine, 23(1), 82-82 (2021-12-23)
Human natural anti-α-galactoside (anti-Gal) and anti-β-glucoside (ABG) antibodies were previously reported to recognize the serine- and threonine-rich peptide sequences (STPS) of albumin-associated O-glycoproteins (AOP1 and AOP2) as surrogate antigens, forming anti-Gal/ABG-AOP1/AOP2-albumin triplet immune complexes in plasma. Since antibodies in these
Holger Husi et al.
Biomedical reports, 10(3), 165-174 (2019-03-25)
Several potential urinary biomarkers exhibiting an association with upper gastrointestinal tumour growth have been previously identified, of which S100A6, S100A9, rabenosyn-5 and programmed cell death 6-interacting protein (PDCD6IP) were further validated and found to be upregulated in malignant tumours. The
Laura Weber et al.
International journal of molecular sciences, 25(7) (2024-04-13)
Despite the understanding of the coronavirus disease-19 (COVID-19), the role of salivary extracellular vesicles (sEVs) in COVID-19 remains unclear. Exploring the proteomic cargo of sEVs could prove valuable for diagnostic and prognostic purposes in assessing COVID-19. The proteomic cargo of
Chie Naito et al.
Molecular genetics and metabolism reports, 39, 101069-101069 (2024-03-22)
Glycogen Storage disease type 4 (GSD4), a rare disease caused by glycogen branching enzyme 1 (GBE1) deficiency, affects multiple organ systems including the muscles, liver, heart, and central nervous system. Here we report a GSD4 patient, who presented with severe
Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling
Gelamo E L, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1594(1), 84-99 (2002)

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