Human Serpin F2/ alpha 2-Antiplasmin Antibody

Catalog # Availability Size / Price Qty
MAB1470
MAB1470-SP
Detection of Mouse Serpin F2/alpha 2-Antiplasmin by Western Blot
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Product Details
Citations (4)
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Human Serpin F2/ alpha 2-Antiplasmin Antibody Summary

Species Reactivity
Human
Specificity
Detects human Serpin F2/ alpha 2‑Antiplasmin in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human Serpin A1, A3, A4, A5, recombinant mouse Serpin C1, D1, F2, or recombinant mouse PEDF is observed.
Source
Monoclonal Mouse IgG2A Clone # 236122
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Serpin F2/ alpha 2‑Antiplasmin
Met28-Lys491
Accession # P08697
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
1 µg/mL
Recombinant Human Serpin F2/ alpha 2‑Antiplasmin (Catalog # 1470-PI)
Immunoprecipitation
25 µg/mL
Conditioned cell culture medium spiked with Recombinant Human Serpin F2/ alpha 2‑Antiplasmin (Catalog # 1470-PI), see our available Western blot detection antibodies

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Western Blot Detection of Mouse Serpin F2/alpha 2-Antiplasmin by Western Blot View Larger

Detection of Mouse Serpin F2/alpha 2-Antiplasmin by Western Blot Proteomics analysis reveals losartan-mediated reversion of early fibrotic changes in RDEBHeat map of cluster analysis of protein abundances determined by label-free quantification mass spectrometry. Extracted ion currents were used to determine protein abundances, and respective intensities were log2-transformed and normalized (z-score). Samples were clustered hierarchically, and protein abundances were clustered by k-means. Cluster sizes are indicated by color code on the left. Clusters 3, 4, 5, 8, and 9 highlight losartan-induced changes. The general patterns of protein abundance in clusters 5, 8, and 9 are similar in wild-type and losartan-treated C7-hypomorphic mice and thus contain downstream targets of losartan involved in RDEB disease progression. WT, wild-type; H, hypomorphic; H + Los, losartan-treated C7-hypomorphic skin.Proteins from cluster 5 carrying GO terms related to inflammation were short-listed and analyzed on potential interactions using default settings in STRING DB (confidence score 0.4) (Szklarczyk et al, 2015).Bar graphs show abundance of selected representative proteins in cluster 5 that were normalized by losartan treatment. Shown to the left are the mean ± S.E.M. of the normalized protein abundance (LFQ intensity) of groups of individual mice corresponding to wild-type, untreated, and losartan-treated C7-hypomorphic mice as indicated in the figure. Unpaired t-test was used to calculate significance. Abundance of Lrg1: *P-value C7-hypomorphic vs. losartan-treated C7-hypomorphic mice = 0.022; abundance of serpin f2: **P-value untreated C7-hypomorphic vs. losartan-treated C7-hypomorphic mice = 0.0084; abundance of vitronectin: **P-value untreated C7-hypomorphic vs. losartan-treated C7-hypomorphic mice = 0.0094. Right, validation of proteomics analysis by Western blotting of independent biological replicates. Representative Western blots of skin lysates from wild-type, untreated C7-hypomorphic, and 7-week losartan-treated C7-hypomorphic mice not used for proteomics. Blots were probed with antibodies against proteins as indicated. Erk1/2 and beta -tubulin served as loading controls. The analysis shows that there is a good correlation between proteomics data and abundance detected by Western blotting (n = 3 per group). Source data are available online for this figure. Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/26194911), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Serpin F2/alpha 2-Antiplasmin

Serpin F2 is a member of the Serpin superfamily and the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots (1, 2). In addition to plasmin, Serpin F2 is also an efficient inhibitor of trypsin and chymotrypsin (3). Liver and kidney are major sites of Serpin F2 production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern of Serpin F2 indicates that it is a key regulator of plasmin-mediated proteolysis in these tissues (4). Human Serpin F2 is synthesized as a 491 amino acid precursor with a 27 amino acid signal peptide. The secreted protein has a short propeptide (residues 28‑39) and a mature chain (residues 40‑491). The presence of the propeptide did not affect its ability to inhibit plasmin but reduced its cross-linking ability to fibrin (5).

References
  1. Tone, M. et al. (1987) J. Biochem. 102:1033.
  2. Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
  3. Potempa, J. et al. (1988) Science 241:699.
  4. Menoud, P.-A. et al. (1996) J. Clin. Invest. 97:2478.
  5. Sumi, Y. et al. (1989) J. Biochem. 106:703.
Entrez Gene IDs
5345 (Human); 18816 (Mouse)
Alternate Names
AAPclade F (alpha-2 antiplasmin; alpha 2-Antiplasmin; Alpha-2-AP; Alpha-2-PI; Alpha-2-plasmin inhibitor; pigment epithelium derived factor), member 2; Serpin F2; serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epitheliumderived factor), member 2

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Citations for Human Serpin F2/ alpha 2-Antiplasmin Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

4 Citations: Showing 1 - 4
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  1. Losartan ameliorates dystrophic epidermolysis bullosa and uncovers new disease mechanisms
    Authors: Nystrom A, Thriene K, Mittapalli V et al.
    EMBO Mol Med.
  2. Temporal Changes in Extracellular Vesicle Hemostatic Protein Composition Predict Favourable Left Ventricular Remodeling after Acute Myocardial Infarction
    Authors: XC Lim, C Huang, SMJM Yatim, SY Chong, SH Tan, X Yang, CL Heldt, J Pedersen, M Talanker, H Modh, MG Wacker, G Pastorin, SP Chan, AM Richards, CJ Charles, MY Chan, JW Wang
    International Journal of Molecular Sciences, 2022-12-25;24(1):.
    Species: Human
    Sample Types: Extracellular Vesicles
    Applications: ELISA Capture
  3. Lowering Low-Density Lipoprotein Particles in Plasma Using Dextran Sulphate Co-Precipitates Procoagulant Extracellular Vesicles
    Authors: JW Wang, YN Zhang, SK Sze, SM van de Weg, F Vernooij, AH Schoneveld, SH Tan, HH Versteeg, L Timmers, CSP Lam, DPV de Kleijn
    Int J Mol Sci, 2017-12-29;19(1):.
    Applications: Bioassay
  4. Extracellular Vesicle Proteins Associated with Systemic Vascular Events Correlate with Heart Failure: An Observational Study in a Dyspnoea Cohort.
    Authors: Zhang Y, Vernooij F, Ibrahim I, Ooi S, Gijsberts C, Schoneveld A, Sen K, den Ruijter H, Timmers L, Richards A, Jong C, Mazlan I, Wang J, Lam C, de Kleijn D
    PLoS ONE, 2016-01-28;11(1):e0148073.
    Species: Human
    Sample Types: Plasma
    Applications: ELISA Development

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