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Recombinant Rat SIRP alpha/CD172a Protein, CF 50 UG

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Recombinant Rat SIRP alpha/CD172a Protein, CF 50 UG信息二維碼

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產(chǎn)品介紹

    基本參數(shù)

    詳細(xì)說明

    • Purity

      >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

    • Endotoxin Level

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

    • Activity

      Measured by the ability of the immobilized protein to support the adhesion of mouse red blood cells.

      The ED50 for this effect is 1.2-4.8 μg/mL.

      Optimal dilutions should be determined by each laboratory for each application.  

    • Source

      Mouse myeloma cell line, NS0-derived Lys32-Asn373, with a C-terminal 6-His tag

    • Accession #

    • N-terminal Sequence    
      Analysis

      Lys32

    • Predicted Molecular Mass

      38.3 kDa

    • SDS-PAGE

      75-95 kDa, reducing conditions

    7307-SA

     

    Formulation Lyophilized from a 0.2 μm filtered solution in PBS.


    Reconstitution Reconstitute at 500 μg/mL in PBS.



    Shipping The product is shipped at ambient temperature. Upon receipt, store it 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.

    • 3 months, -20 to -70 °C under sterile conditions after reconstitution.


    Background: SIRP alpha/CD172a

    Signal regulatory protein alpha (SIRP alpha, designated CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), is a homodimeric, 100 ? 120 kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily (1 ? 6). SIRPs are paired receptors, with similar extracellular domains but differing C-termini and functions (1, 2). The 509 amino acid (aa) rat SIRP alpha contains a 342 aa extracellular domain (ECD) with one V-type and two C1 type Ig domains and many potential N-glycosylation sites. It has a 113 aa cytoplasmic sequence with ITIM motifs that recruit tyrosine phosphatases SHP-1 and SHP-2 when phosphorylated (6). Rat SIRP alpha ECD shares 60% and 75% aa sequence identity with human and mouse SIRP alpha, respectively. Mouse and human SIRP alpha have at least 30 described polymorphisms, including the human SIRP alpha prominent variant BIT (Brain Ig like molecule with Tyrosine-based activation motifs, also called SIRP alpha 2 or PTPNS) (2). Less is known about rat SIRP alpha polymorphisms and family members. SIRP alpha is expressed mainly on myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells (3 ? 7). It is also found on neurons, smooth muscle and endothelial cells (8 ? 10). SIRP alpha shows adhesion to the ubiquitous CD47/IAP (integrin associated protein) (1, 2). Interaction between SIRP alpha and CD47 on red blood cells occurs in a species specific manner (17). Mouse and human SIRP alpha are allelic in nature, and variations in the V-type Ig?like domain likely impacts its binding to CD47 (11). SIRP alpha engagement generally produces a negative regulatory signal (4). Low SIRP alpha recognition of CD47, which occurs on aged erythrocytes or platelets or xenogenic cells, promotes clearance of CD47low cells from circulation (12-14). SIRP alpha recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production (15). The CD47 integrin-SIRP alpha interaction is reported to promote macrophage fusion during osteoclastogenesis (16).

    • References:

      1. Barclay, A.N. (2009) Curr. Opin. Immunol. 21:47.

      2. van Beek, E.M. et al. (2005) J. Immunol. 175:7781.

      3. Liu, Y. et al. (2005) J. Biol. Chem. 280:36132.

      4. Sano, S-I. et al. (1999) Biochem. J. 344:667.

      5. Lee, W.Y. et al. (2010) J. Biol. Chem. 285:37953.

      6. Fujioka, Y. et al. (1996) Mol. Cell. Biol. 16:6887.

      7. Miyashita, M. et al. (2004) Mol. Biol. Cell 15:3950.

      8. Wang, X.X. & K.H. Pfenninger (2005) J. Cell Sci. 119:172.

      9. Maile, L.A. et al. (2003) Mol. Biol. Cell 14:3519.

      10. Johansen, M.L. & E.J. Brown (2007) J. Biol. Chem. 282:24219.

      11. Takenaka, K. et al. (2007) Nat. Immunol. 8:1313.

      12. Ishikawa-Sekigami, T. et al. (2006) Biochem. Biophys. Res. Commun. 343:1197.

      13. Olsson, M. et al. (2005) Blood 105:3577.

      14. Ide, K. et al. (2007) Proc. Natl. Acad. Sci. USA 104:5062.

      15. Gardai, S.J. et al. (2003) Cell 115:13.

      16. Lundberg, P. et al. (2007) Biochem. Biophys. Res. Commun. 352:444.

      17. Subramanian et al. (2006) Blood 107:2548.

    • Long Name:

      Signal-regulatory Protein alpha

    • Entrez Gene IDs:

      140885 (Human); 19261 (Mouse); 25528 (Rat); 101926317 (Cynomolgus Monkey)

    • Alternate Names:

      BIT; BITbrain-immunoglobulin-like molecule with tyrosine-based activation motifs; Brain Ig-like molecule with tyrosine-based activation motifs; CD172 antigen-like family member A; CD172a antigen; CD172a; Inhibitory receptor SHPS-1; Macrophage fusion receptor; MFR; MFRtyrosine phosphatase SHP substrate 1; MyD-1 antigen; MYD1; MYD-1; P84; protein tyrosine phosphatase, non-receptor type substrate 1; PTPNS1; SHP substrate 1; SHPS1; SHPS-1; SHPS1CD172A; signal-regulatory protein alpha; Signal-regulatory protein alpha-1; Signal-regulatory protein alpha-2; Signal-regulatory protein alpha-3; SIRP alpha; SIRPA; SIRPalpha; Sirp-alpha-1; SIRPalpha2; Sirp-alpha-2; Sirp-alpha-3; SIRPtyrosine-protein phosphatase non-receptor type substrate 1








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