Rat Alpha-1-Antiproteinase (SERPINA1) Protein

Este producto es parte de SERPINA1 - serpin family A member 1
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312€ (20 µg)

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935106861
info@markelab.com
name
Rat Alpha-1-Antiproteinase (SERPINA1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx694319
tested applications
SDS-PAGE

Description

Rat Alpha-1-Antiproteinase (SERPINA1) Protein is a recombinant Rat protein expressed in HEK293 cells.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Host
HEK293 cells
Origin
Rat
Observed MW
Molecular Weight: Calculated MW: 45.1 kDa  Observed MW (SDS-PAGE): 50 kDa
Sequence Fragment: Met1-Arg411
Tag: C-terminal His tag
Expression
Recombinant
Purity
>95% (SDS-PAGE)
Size 1
20 µg
Size 2
100 µg
Form
Lyophilized Reconstitute in sterile H2O. Do not vortex.
Tested Applications
SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 5% - 8% Trehalose, Mannitol and 0.01% Tween-80.
Availability
Shipped within 5-15 working days.
Storage
Store lyophilized between -20 °C and -80 °C.
Dry Ice
No
UniProt ID
P17475
Alias
PI,A1A,AAT; PI1,A1AT,nNIF,PRO2275,alpha1AT,Alpha-1-antitrypsin,Alpha-1 protease inhibitor,Alpha-1-antiproteinase,Serpin A1
Background
Protein SERPINA1
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

The SERPINA1 gene, commonly known as alpha-1 antitrypsin (A1AT), encodes a protein that plays a crucial role in protecting tissues from enzymes of inflammatory cells, particularly neutrophil elastase. This gene is part of the serine protease inhibitor (serpin) superfamily and is located on chromosome 14 (14q32.13). Alpha-1 antitrypsin is primarily synthesized in the liver, although it is also produced in smaller quantities by other tissues, including the lungs, intestines, and kidneys. The protein encoded by SERPINA1 is a glycoprotein that circulates in the blood and functions as a major inhibitor of proteases, especially neutrophil elastase, which, if left unchecked, can degrade elastin and other extracellular matrix components, leading to tissue damage.

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