A8273
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
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), ODD
Species reactivity:
human
Citations:
111
Technique(s):
Ouchterlony double diffusion: suitable, indirect ELISA: 1:4,000-1:6,000
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)
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.
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.
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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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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)
Hiroshi Watanabe et al.
Acta histochemica et cytochemica, 50(3), 111-118 (2017-07-27)
Long-term submandibular duct obstruction is thought to cause irreversible atrophy and dysfunction of the submandibular gland. As an atrophic gland may be induced clinically by chronic or recurrent infection, it is generally removed surgically. However, the regenerative capacity of atrophic
Lamin A/C Maintains Exocrine Pancreas Homeostasis by Regulating Stability of RB and Activity of E2F.
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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