Recombinant Rat Serpin A12 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8339-PI

R&D Systems, part of Bio-Techne
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8339-PI-050
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Key Product Details

Source

NS0

Accession #

Q8R4Z1

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Serpin A12 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived rat Serpin A12 protein
Leu20-Pro411, with a C-terminal 10-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Leu20

Predicted Molecular Mass

47 kDa

SDS-PAGE

45-54 kDa, reducing conditions

Activity

Measured by its ability to inhibit KLK7 cleavage the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002).
The IC50 is <45 nM, as measured under the described conditions.

Formulation, Preparation and Storage

8339-PI
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Serpin A12

Serpin A12, also known as Vaspin, is a 45-50 kDa secreted adipokine that contributes to the maintenance of insulin sensitivity (1, 2). It is structurally related to the Serpin family of serine protease inhibitors (3). Mature rat Serpin A12 shares 62% and 88% amino acid sequence identity with human and mouse Serpin A12, respectively (3). It is expressed by adipocytes in visceral and subcutaneous fat, in the gastric glands and epithelium, and in the placenta (3-5). Serpin A12 circulates in a complex with Kallikrein 7, and it prevents the Kallikrein 7 mediated cleavage of Insulin (6). It promotes the elevation of circulating insulin and improves glucose tolerance but can also inhibit the high glucose induced activation of the Insulin Receptor (3, 6, 7). Serpin A12 inhibits TRANCE/RANK L induced osteoclast development and the inflammatory activation of vascular smooth muscle and endothelial cells (7-9). It additionally functions as an anti-apoptotic protein in vascular endothelial cells and osteoblasts (10, 11).

References

  1. Choi, S.H. et al. (2013) Front. Endocrinol. (Lausanne) 4:97.
  2. Goktas, Z. et al. (2013) Front. Endocrinol. (Lausanne) 4:69.
  3. Hida, K. et al. (2005) Proc. Natl. Acad. Sci. USA 102:10610.
  4. Lee, J.A. et al. (2011) Endocr. J. 58:639.
  5. Caminos, J.E. et al. (2009) Histol. Histopathol. 24:979.
  6. Heiker, J.T. et al. (2013) Cell Mol. Life Sci. 70:2569.
  7. Li, H. et al. (2013} Atherosclerosis 228:61.
  8. Kamino, N. et al. (2013) Connect. Tissue Res. 54:147.
  9. Jung, C.H. et al. (2014) Cardiovasc. Diabetol. 13:41.
  10. Jung, C.H. et al. (2011) Biochem. Biophys. Res. Commun. 413:264.
  11. Zhu, X. et al. (2013) Amino Acids 44:961.

Alternate Names

OL-64, Vaspin

Entrez Gene IDs

145264 (Human); 68054 (Mouse); 191570 (Rat)

Gene Symbol

SERPINA12

UniProt

Q8R4Z1

Additional Serpin A12 Products

Product Documents for Recombinant Rat Serpin A12 Protein, CF

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Product Specific Notices for Recombinant Rat Serpin A12 Protein, CF

For research use only

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