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Key Documents

A8273

Sigma-Aldrich

Anti-α-Amylase antibody produced in rabbit

fractionated antiserum, lyophilized powder

Synonyme(s) :

Alpha Amylase Antibody, Alpha Amylase Antibody - Anti-α-Amylase antibody produced in rabbit

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About This Item

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

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

fractionated antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

lyophilized powder

Espèces réactives

human

Conditionnement

vial of 2 mL lyophilized antiserum

Technique(s)

Ouchterlony double diffusion: suitable
indirect ELISA: 1:4,000-1:6,000

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... AMY1A(276)

Description générale

α-amylase is primarily produced in abundance in the salivary glands and pancreas. The expression is also seen in jejunum and mammary glands. The genes encoding α-amylase are AMY1 and AMY2 located in the short arm of chromosome 1. AMY1 is responsible for producing the enzyme in saliva and mammary gland and AMY2 produces the enzyme synthesized in the pancreas. The expression of AMY1 occurs also in certain tumour tissues. Mammalian amylases are composed of three structural domains (A, B and C). Domain A contains the active site with two aspartate and one glutamate residue. Domain B borders the active site region and is essential for maintaining the protein conformation. Domain C is involved in catalytic mechanism.

Spécificité

The antiserum is specific for human a-amylase found in human saliva and human pancreatic extract. No reaction with other human saliva proteins or pancreatic extract proteins is observed.

Immunogène

human salivary α-amylase.

Application

Anti-α-Amylase antibody produced in rabbit has also been used in immunocytochemistry analysis.
Anti-a-Amylase antibody produced in rabbit has been used in immunofluorescence and immunohistochemical analysis.
Mouse pancreatic sections were fixed in 4% paraformaldehyde and used for immunohistochemistry using rabbit anti-amylase antibody at a dilution of 1:100.

Actions biochimiques/physiologiques

α-Amylase is essential for catalyzing the primary step in starch digestion, a main source of carbohydrate in the human diet. α-amylase hydrolysis the polysaccharide with the ultimate production of maltose, maltotriose and limit dextrins as the main products.

Forme physique

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Reconstitution

Reconstitute with 2 mL deionized water.

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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Human alpha-amylase and starch digestion: An interesting marriage
Butterworth PJ, et al.
Starch/Staerke, 63(7), 395-405 (2011)
Maho Kodama et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 56(1), 33-44 (2007-09-19)
In this study, we describe pancreatic cell ontogeny in renal capsule-transplanted embryonic stem cells (ES) after injury by streptozocin (STZ), showing pancreatogenesis in situ. Seven-week-old female BALB/c nude mice were treated with either a single 175- or 200-mg/kg STZ dose
Imane Song et al.
PloS one, 10(10), e0140148-e0140148 (2015-10-10)
One week of treatment with EGF and gastrin (EGF/G) was shown to restore normoglycemia and to induce islet regeneration in mice treated with the diabetogenic agent alloxan. The mechanisms underlying this regeneration are not fully understood. We performed genetic lineage
Angela Criscimanna et al.
Gastroenterology, 147(5), 1106-1118 (2014-08-17)
Although the cells that contribute to pancreatic regeneration have been widely studied, little is known about the mediators of this process. During tissue regeneration, infiltrating macrophages debride the site of injury and coordinate the repair response. We investigated the role
Rami Khoriaty et al.
Molecular biology of the cell, 28(15), 2146-2154 (2017-05-26)
Mice with germline absence of SEC23B die perinatally, exhibiting massive pancreatic degeneration. We generated mice with tamoxifen-inducible, pancreatic acinar cell-specific

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