Human Aspartate Aminotransferase, Cytoplasmic / AST (GOT1) Protein

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221€ (10 µg)

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935106861
info@markelab.com
name
Human Aspartate Aminotransferase, Cytoplasmic / AST (GOT1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx065466
tested applications
WB, SDS-PAGE

Description

Human Aspartate Aminotransferase (AST) is a recombinant Human protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Immunogen Target
Aspartate Aminotransferase, Cytoplasmic / AST (GOT1)
Host
E. coli
Assay Type
Activity: Not tested
Sequence Fragment: Met1-Gln413
Tag: N-terminal His tag
Origin
Human
Conjugation
Unconjugated
Observed MW
Calculated MW: 47.8 kDa  Observed MW (SDS-PAGE): 44 kDa
Expression
Recombinant
Purity
> 97%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 0.01% Sarcosyl, 5% Trehalose.
Availability
Shipped within 5-7 working days.
Storage
Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles.
Dry Ice
No
UniProt ID
P17174
Gene ID
2805
NCBI Accession
NP_002070.1
Alias
cAspAT,Transaminase A
Background
Protein GOT1
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.
To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Concentration: Prior to lyophilization: 800 µg/ml

Descripción

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