Reactivity | RtSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | 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 rat SIRP alpha/CD172a protein Lys32-Asn373, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Lys32 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Sirpa |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 38.3 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 | 75-95 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 500 μg/mL in PBS. |
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).
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