Human Serpin A12 (SERPINA12) Protein

Este producto es parte de SERPINA12 - serpin family A member 12
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221€ (10 µg)

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935106861
info@markelab.com
name
Human Serpin A12 (SERPINA12) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx069668
tested applications
WB, SDS-PAGE

Description

Human Serpin A12 (SERPINA12) is a recombinant Human protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Serpin A12 (SERPINA12)
Host
E. coli
Assay Type
Activity: Not tested
Sequence Fragment: Asn52-Arg143
Tag: N-terminal His tag
Origin
Human
Conjugation
Unconjugated
Observed MW
Calculated MW: 12.1 kDa
Expression
Recombinant
Purity
> 95%
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: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
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
Q8IW75
Alias
Serpin A12,OL-64,Visceral adipose tissue-derived serine protease inhibitor,Vaspin,Visceral adipose-specific serpin
Background
Protein SERPINA12
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 PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, 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: 200 µg/ml

Descripción

SERPINA12, also known as Vaspin (Visceral adipose tissue-derived serpin), is a member of the serpin (serine protease inhibitor) superfamily, which is widely recognized for its role in inhibiting serine proteases. Vaspin was first identified in 2005 in the visceral adipose tissue of Otsuka Long-Evans Tokushima Fatty (OLETF) rats, an animal model of obesity and type 2 diabetes. The discovery of Vaspin was driven by the need to understand better the molecular mechanisms linking obesity, insulin resistance, and metabolic syndrome. Since then, Vaspin has been studied extensively for its role in metabolism, inflammation, and potential therapeutic applications in treating metabolic diseases.

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