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Key Documents

A8273

Sigma-Aldrich

Anti-α-Amylase antibody produced in rabbit

fractionated antiserum, lyophilized powder

Synonym(s):

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

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About This Item

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

biological source

rabbit

Quality Level

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

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.

Specificity

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.

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.

Physical form

Lyophilized from 0.01 M phosphate buffered saline, pH 7.2

Reconstitution

Reconstitute with 2 mL deionized water.

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Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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