Ugrás a tartalomra
Merck

A8273

Sigma-Aldrich

Anti-α-Amylase antibody produced in rabbit

fractionated antiserum, lyophilized powder

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.46

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

fractionated antiserum

antitest terméktípus

primary antibodies

klón

polyclonal

form

lyophilized powder

faj reaktivitás

human

kiszerelés

vial of 2 mL lyophilized antiserum

technika/technikák

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

tárolási hőmérséklet

2-8°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... AMY1A(276)

Általános leírás

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.

Egyediség

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.

Immunogen

human salivary α-amylase.

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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.

Fizikai forma

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Feloldás

Reconstitute with 2 mL deionized water.

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Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
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
Ultrastructural analysis of pancreatic acinar cells from mice fed on genetically modified soybean
Malatesta M, et al.
Journal of Anatomy, 201(5), 409-415 (2002)
Human alpha-amylase and starch digestion: An interesting marriage
Butterworth PJ, et al.
Starch/Staerke, 63(7), 395-405 (2011)
Jared S Elenbaas et al.
Gastroenterology, 154(6), 1625-1629 (2018-01-26)
Lamins have important roles in nuclear structure and cell signaling. Several diseases are associated with mutations in the lamin A/C gene (LMNA in humans). Patients with familial partial lipodystrophy caused by LMNA mutations develop pancreatitis, but lamin function in the

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