Rat Serpin A12 (SERPINA12) Protein
234€ (10 µg)
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935106861
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name
Rat Serpin A12 (SERPINA12) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx069670
tested applications
WB, SDS-PAGE
Description
Recombinant Serpin A12 (SERPINA12) is a recombinant Rat protein produced in a Prokaryotic expression system (E. coli).
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Serpin A12 (SERPINA12) |
| Host | E. coli |
| Origin | Rat |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 12.1 kDa Observed MW (SDS-PAGE): 10 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Asn52-Arg143 Tag: N-terminal His tag |
| Purity | > 97% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized 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 10 mM PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in 10 mM 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. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 5% Trehalose. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q8R4Z1 |
| 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 human consumption, cosmetic, therapeutic or diagnostic use. |
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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