Skip to main content

Recombinant Human SIRP delta Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 10138-SB

R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
Loading...
10138-SB-050

Key Product Details

Source

HEK293

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human SIRP delta protein
Human SIRP delta
(Phe30-Arg197)
Accession # Q9H106
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

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

N-terminal Sequence Analysis

Phe30

Predicted Molecular Mass

45 kDa

SDS-PAGE

50-60 kDa, under reducing conditions

Activity

Measured by its binding ability in a functional ELISA.
When Recombinant Human SIRP delta Fc Chimera (Catalog # 10138-SB) is immobilized at 1 µg/mL (100 µL/well), recombinant human DIRAS2 binds with an ED50 of 0.15-0.9 μg/mL.

Scientific Data Images for Recombinant Human SIRP delta Fc Chimera Protein, CF

Recombinant Human SIRP delta Fc Chimera Protein Binding Activity

Recombinant Human SIRP delta Fc Chimera Protein Binding Activity

When Recombinant Human SIRP delta Fc Chimera (Catalog # 10138-SB) is immobilized at 1 µg/mL, recombinant human DIRAS2 binds with an ED50 of 0.15-0.9 μg/mL.
Recombinant Human SIRP delta Fc Chimera Protein SDS-PAGE

Recombinant Human SIRP delta Fc Chimera Protein SDS-PAGE

2 μg/lane of Recombinant Human SIRP delta Fc Chimera (Catalog # 10138-SB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 50-60 kDa and 100-120 kDa, respectively.

Formulation, Preparation and Storage

10138-SB
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 delta

SIRPD (Signal Regulatory Protein Delta), also know as Protein Tyrosine Phosphatase non-Receptor Type Substrate 1-l Like 2 (PTPNS1L2), is member of the signal regulatory proteins (SIRPS) family (1). SIRPD contains a 168 amino acid Ig-like domain that is characteristic of other SIRP family members (1). Unlike other members of SIRPS family, SIRPD lacks the transmemberane region, and is secreted (2). Murine homologs of SIRPD are not characterized. Expression sequence tag analysis suggests that SIRPD may be expressed in sperm cells and respiratory tissue (2). Using BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) high-throughput affinity purification–mass spectrometry (AP–MS) analysis to identify probable protein–protein interactions, several candidate SIRPD interactions were found including DIRAS2 (3). In-house testing indicates SIRPD can interact with DIRAS2.

References

  1. Van den Berg, T.K. et al. (2005) J. Immunol. 175:7788.
  2. Van Beek, E.M. et al. (2005) J Immunol. 175:7781.
  3. Huttlin, E.L. et al. (2017) Nature 545:505.

Long Name

Signal-regulatory Protein delta

Alternate Names

dJ576H24.4, PTPNS1L2, SIRP-Delta, SIRPD

Entrez Gene IDs

128646 (Human)

Gene Symbol

SIRPD

UniProt

Additional SIRP delta Products

Product Documents for Recombinant Human SIRP delta Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human SIRP delta Fc Chimera Protein, CF

For research use only

Loading...
Loading...
Loading...