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Merck
Összes fotó(10)

Fontos dokumentumok

HPA000927

Sigma-Aldrich

Anti-SERPINA1 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Szinonimák:

Anti-Alpha-1 protease inhibitor, Anti-Alpha-1-antiproteinase, Anti-Alpha-1-antitrypsin precursor, Anti-SPAAT

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
Human Protein Atlas-szám:
NACRES:
NA.43
konjugátum:
unconjugated
application:
IF
IHC
klón:
polyclonal
faj reaktivitás:
human
citations:
6
technika/technikák:
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:2500-1:5000

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

termékcsalád

Prestige Antibodies® Powered by Atlas Antibodies

Forma

buffered aqueous glycerol solution

faj reaktivitás

human

fejlettebb validálás

orthogonal RNAseq
independent
Learn more about Antibody Enhanced Validation

technika/technikák

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:2500-1:5000

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... SERPINA1(5265)

Általános leírás

SERPINA1 (serpin peptidase inhibitor, clade A, member 1), also called α1-antitrypsin, is an acute-phase glycoprotein, which belongs to the serpin superfamily. It is predominantly found in the plasma, and is secreted by hepatocytes. This gene is localized to human chromosome 14q32.1, and is composed of four coding and three non-coding exons.

Immunogén

α-1-antitrypsin precursor recombinant protein epitope signature tag (PrEST)

Sequence
HDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYGAPHR

Alkalmazás

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biokémiai/fiziológiai hatások

α-1 Antitrypsin (A1AT or AAT) is a serine proteinase inhibitor with potent anti-inflammatory, anti-apoptotic, antimicrobial and cytoprotective activities. In humans, it could be a potential novel therapeutic drug for the protection against neurodegeneration after ischemic stroke. Its deficiency is associated with an increased risk for lung and liver disease.

Tulajdonságok és előnyök

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Kapcsolódás

Corresponding Antigen APREST82416

Fizikai forma

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Jogi információk

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Jogi nyilatkozat

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Huong L Moldthan et al.
Journal of stroke and cerebrovascular diseases : the official journal of National Stroke Association, 23(5), e355-e363 (2014-03-04)
Our objective is to develop a new therapy for the treatment of stroke. Currently, the only effective therapy for acute ischemic stroke is the thrombolytic agent recombinant tissue plasminogen activator. α1-Antitrypsin (AAT), a serine proteinase inhibitor with potent anti-inflammatory, anti-apoptotic
Brenda B Suh-Lailam et al.
American journal of clinical pathology, 141(5), 742-746 (2014-04-10)
α1-Antitrypsin (AAT) deficiency is associated with an increased risk for lung and liver disease. Identification of AAT deficiency as the underlying cause of these diseases is important in correct patient management. AAT deficiency is commonly diagnosed by demonstrating low concentrations
Chae Hwa Kwon et al.
Oncotarget, 6(24), 20312-20326 (2015-05-28)
The role of Snail and serpin peptidase inhibitor clade A member 1 (serpinA1) in tumorigenesis has been previously identified. However, the exact role and mechanism of these proteins in progression of colorectal cancer (CRC) are controversial. In this study, we
C H Kwon et al.
British journal of cancer, 111(10), 1993-2002 (2014-09-12)
In a previous study, we reported that serpin peptidase inhibitor clade A member 1 (serpinA1) is upregulated in Snail-overexpressing gastric cancer. Although serpinA1 has been studied in several types of cancer, little is known about its roles and mechanisms of
James A Irving et al.
The Biochemical journal, 468(1), 99-108 (2015-03-05)
A monoclonal antibody (mAb) that binds to a transient intermediate may act as a catalyst for the corresponding reaction; here we show this principle can extend on a macro molecular scale to the induction of mutant-like oligomerization in a wild-type

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