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Merck

A8273

Anti-α-Amylase antibody produced in rabbit

fractionated antiserum, lyophilized powder

동의어(들):

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

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), ODD
Citations:
111
기술 서비스
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도움 문의

biological source

rabbit

conjugate

unconjugated

antibody form

fractionated antiserum

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

human

packaging

vial of 2 mL lyophilized antiserum

technique(s)

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

storage temp.

2-8°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... AMY1A(276)

General description

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.

Immunogen

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.

Biochem/physiol Actions

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.
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.

Physical form

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Preparation Note

Reconstitute with 2 mL deionized water.

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저장 등급

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Lot/Batch Number

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문서 라이브러리 방문

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
Human alpha-amylase and starch digestion: An interesting marriage
Butterworth PJ, et al.
Starch/Staerke, 63(7), 395-405 (2011)
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)
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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