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Merck

A1151

Sigma-Aldrich

Anti-Albumin antibody produced in goat

fractionated antiserum, lyophilized

Sinónimos:

Albumin Detection Antibody, Anti-Albumin, Goat Anti-Albumin

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

Quality Level

recombinant

expressed in goat

antibody form

fractionated antiserum

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized

mol wt

antigen 65 kDa

species reactivity

human

packaging

vial of 2 mL lyophilized antiserum

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... ALB(213)

General description

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. 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.
Goat polyclonal anti-Albumin antiserum is immunospecific for human albumin by immunoelectrophoresis against normal human serum and human albumin. Identity and purity of the specific antibody is established by immunoelectrophoresis (IEP). Electrophoresis of the antiserum followed by diffusion against anti-goat serum results in multiple arcs of precipitation, whereas against anti-goat IgG, it results in a single arc of precipitation in the γ region.

Immunogen

purified human albumin

Application

Goat polyclonal anti-Albumin antiserum is used to tag albumin for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of albumin a variety of clinical indications.

Physical form

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Disclaimer

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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Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Tetsu Akimoto et al.
American journal of physiology. Cell physiology, 284(6), C1625-C1632 (2003-02-28)
We have demonstrated that during culture under 5% O(2,) the addition of recombinant human VEGF or FGF2 to mouse embryonic aorta explants (thoracic level to lateral vessels supplying the mesonephros and metanephros) stimulates microvessel formation. Here we show that microvessel
G Grossmann et al.
Journal of applied physiology (Bethesda, Md. : 1985), 82(6), 2003-2010 (1997-06-01)
Near-term newborn rabbits were exposed via the airways to a monoclonal antibody to surfactant protein B and ventilated for 0-120 min. Control animals received nonspecific rabbit or mouse immunoglobulin G, saline, or no material via the airways. Administration of the
Tetsu Akimoto et al.
Organogenesis, 2(1), 17-21 (2005-01-01)
Hypoxia exists widely in developing embryos where it may regulate blood vessel formation. VEGF and FGF2 produced in developing renal primordia (metanephroi) stimulate microvessel formation from embryonic thoracic aorta cultured under hypoxic conditions (HC) relative to room air (RA). The
Elliott L Rodriguez et al.
Journal of chromatography. A, 1638, 461683-461683 (2020-11-24)
Diabetes is characterized by elevated levels of blood glucose, which can result in the modification of serum proteins. The modification of a protein by glucose, or glycation, can also lead to the formation of advanced glycated end-products (AGEs). One protein
Mischa R Müller et al.
mAbs, 4(6), 673-685 (2013-05-17)
Advances in recombinant antibody technology and protein engineering have provided the opportunity to reduce antibodies to their smallest binding domain components and have concomitantly driven the requirement for devising strategies to increase serum half-life to optimise drug exposure, thereby increasing

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