Recombinant Mouse GASP-1/WFIKKN2 Protein

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Recombinant MouseGASP‑1/WFIKKN2 (Catalog # 9956-GS) dose dependently inhibits Recombinant Human/Mouse/RatGDF‑8/Myostatin (Catalog # 788-G8) activity in the K562 human chronic myelogenous leukemia cell line. ...read more

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Recombinant Mouse GASP-1/WFIKKN2 Protein Summary

Details of Functionality
Measured by its ability to inhibit rmGDF-8 activity in K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 0.02-0.12 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse GASP-1/WFIKKN2 protein
Met1-Gln571, With a C-Terminal 6-His tag
Accession #
N-terminal Sequence
Leu30
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
61 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
63-77 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse GASP-1/WFIKKN2 Protein

  • GASP1
  • GASP-1
  • Growth and differentiation factor-associated serum protein 1
  • hGASP-1
  • WAP, follistatin, immunoglobulin, kunitz and NTR domain-containing-relatedprotein
  • WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 2
  • WAP, FS, Ig, two KU and NTR module related protein
  • WAP, kazal, immunoglobulin, kunitz and NTR domain-containing protein 2
  • WFIKKN2
  • WFIKKN-related protein
  • WFIKKNRP
  • WFIKKNRPmultivalent protease inhibitor protein

Background

Growth and differentiation factor-associated serum protein 1 (GASP-1), also known as WAP, Follistatin/Kazal, Immunoglobulin, Kunitz and Netrin domain containing protein 2 (WFIKKN2), appears to be a multifunctional molecule comprised of several conserved domains. GASP-1, along with the highly related GASP-2 (WFIKKN1), contains a WAP domain, a Follistatin/Kazal domain, an Immunoglobulin domain, two Kunitz‐type protease inhibitor domains and a netrin domain (1). GASP-1 was first isolated in a screen to identify proteins in mice that copurify with Myostatin (GDF8) (1). Mature mouse GASP-1 is 542 amino acids (aa) and shares 94% and 98% aa identity with mature human and rat GASP-1, respectively.

WAP, Follistatin, Kazal and Netrin domains are all implicated in protease inhibition, and GASP-1 and 2 may be protease inhibitor proteins involved in muscle development (1). In humans, GASP-1 and 2 show distinct expression patterns, with GASP-1 expression during development highest in the brain, skeletal muscle, thymus and kidney (2). In mice, GASP-1 expression can be detected in the neural tube and limb buds of developing embryos, while in adult mice it is found in numerous tissue types (3, 4). Both GASP-1 and 2 appear to bind several members of the TGF beta family with high affinity, including Activin, BMP2, BMP4, TGF-beta 1, GDF-8 and GDF-11 (1, 5, 6). Interestingly, GASP-1 has been shown to specifically inhibit the activity of GDF-8 and GDF-11 but not the other TGF-beta family proteins (1, 4, 6). GASP-1 binds directly but independently to both mature myostatin and the myostatin propeptide (1). Over expression of GASP-1 in mice results in animals that are hyper muscled, consistent with reduction in GDF-8 signaling (7).

  1. Hill, J.J. et al. (2003) Mol. Endo. 17:1144.
  2. Trexler, M. et al. (2002) Biol. Chem. 383:223.
  3. Monestier, O. et al. (2012) PLoS One 7(8):e43710.
  4. Lee, Y and Lee S. (2013) PNAS 110(39).
  5. Kondas, K. et al. (2008) JBC 283:23677.
  6. Szlama, G. et al. (2010) FEBS J 277:5040.
  7. Monestier, O. et al. (2012) BMC Genomics 13(1):541.

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