SIRP alpha Active Protein | SIRPA active protein

SIRP alpha, Recombinant, Human (SIRPa, Signal Regulatory Protein, SHPS-1, BIT, p84, CD172a)

Cat. Num. AAA637456

• Gene Names: SIRPA; BIT; MFR; P84; SIRP; MYD-1; SHPS1; CD172A; PTPNS1
• Purity: Highly Purified; 90%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain.
• Synonyms: SIRP alpha; Recombinant; Human (SIRPa; Signal Regulatory Protein; SHPS-1; BIT; p84; CD172a); SIRPA active protein

• Host: Recombinant Human
• Purity/Purification: Highly Purified; 90%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain.
• Form/Format: Supplied as a lyophilized powder in PBS, pH 7.4.

• Activity: Measured by the ability of the immobilized protein to support the adhesion of red blood cells (Subramanian S., et al., 2006, Blood 107:2548-2556).
• Endotoxin Level: 1EU/1ug.
• Reconstitute: Reconstitute with 500ul sterile PBS.
• N-terminal Sequence Analysis: Gly27 and Glu31
• SDS-PAGE: 70-105kD, reducing conditions.
• Activity: Measured by the ability of the immobilzed protein to support the adhesion of red blood cells (Subramanian S., et al., 2006, Blood 107: 2548-2556). Red blood cells added at 10x 10e6 cells/ml (100ul/well) to SIRPa coated plated will adhere after 1 hour at 37 degree C. The ED50 for this effect is 0.6-2.4ug/ml
• Preparation and Storage: Lyophilized powder may be stored at -20 degree C. Stable for 12 months after receipt at -20 degree C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Reconstituted product is stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for SIRPA active protein

Signal regulatory protein alpha (SIRPA, designated CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), is a monomeric ~90kD type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily.1-4 SIRPs are paired receptors, with similar extracellular domains but differing C-termini and functions.1, 2 The 503 amino acid (aa) human SIRPA contains a 342 aa extracellular domain (ECD), with one V-type, and two C1-type Ig domains, and three potential N-glycosylation sites. It has a 110 aa cytoplasmic sequence with ITIM motifs that recruit tyrosine phosphatases SHP-1 and SHP-2 when phosphorylated.4 Human SIRPA has more than 40 described polymorphisms, including the prominent BIT (Brain Ig-like molecule with Tyrosine-based activation motifs, also called SIRPA2 or PTPNS).5 One reported isoform lacks aa 1-101, which eliminates most of the V-type Ig domain. Human SIRPA ECD shares 61%, 60%, 71%, 72% and 73% aa identity with mouse, rat, porcine, bovine and equine SIRPA, respectively; it shares 84% and 76% aa identity with human SIRPB1 and SIRPy, respectively.2 SIRPA is expressed mainly on myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells.3-6 It is also found on neurons, smooth muscle and endothelial cells.7-9 SIRPA shows adhesion to the ubiquitous CD47/IAP (integrin-associated protein), while SIRPY binds more weakly and SIRPA1 does not bind at all.1, 2 Mouse and human SIRPA-CD47 binding only cross-reacts for specific polymorphisms and influences engraftment of xenotransplanted stem cells.6, 10 SIRPA engagement generally produces a negative regulatory signal.4 Low SIRPA recognition of CD47, which occurs on aged erythrocytes or platelets or xenogenic cells, promotes clearance of CD47low cells from circulation.11-13 SIRPA Arecognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production.14 CD47- integrin-SIRPA interaction is reported to promote macrophage fusion during osteoclastogenesis.15

A DNA sequence encoding the extracellular domain of human SIRP (Gly 27-Arg 370; Accession # NP_542970) was fused to the Fc region of human IgG1 via a polypeptide linker. The chimeric protein was expressed in Chinese hamster ovary cells.
Calculated molecular mass of ~ 64kD. As a result of glycosylation, the recombinant protein migrates as an ~ 70-105kD protein in SDS-PAGE under reducing conditions.

Product Categories/Family for SIRPA active protein

Molecular Biology; MB-Protein Kinase Substrates

NCBI and Uniprot Product Information

• NCBI GI #: 49899261
• NCBI GeneID: 140885
• UniProt Accession #: P78324; O00683; O43799; Q8N517; Q8TAL8; Q9H0Z2; Q9UDX2; Q9UIJ6; Q9Y4U9; A2A2E1; A8K411; B2R6C3
• Molecular Weight: 54,967 Da
• NCBI Official Full Name: Signal-regulatory protein alpha
• NCBI Official Synonym Full Names: signal-regulatory protein alpha
• NCBI Official Symbol: SIRPA
• NCBI Official Synonym Symbols: BIT; MFR; P84; SIRP; MYD-1; SHPS1; CD172A; PTPNS1
• NCBI Protein Information: tyrosine-protein phosphatase non-receptor type substrate 1; myd-1 antigen; inhibitory receptor SHPS-1; macrophage fusion receptor; CD172 antigen-like family member A; tyrosine phosphatase SHP substrate 1; brain-immunoglobulin-like molecule with tyrosine-based activation motifs
• UniProt Protein Name: Tyrosine-protein phosphatase non-receptor type substrate 1
• Protein Family: Tyrosine-protein phosphatase non-receptor
• UniProt Gene Name: SIRPA
• UniProt Synonym Gene Names: BIT; MFR; MYD1; PTPNS1; SHPS1; SIRP; SHP substrate 1; SHPS-1; Bit; Sirp-alpha-1; Sirp-alpha-2
• UniProt Entry Name: SHPS1_HUMAN

NCBI Description

The protein encoded by this gene is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. This protein can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and serve as substrates of PTPs. This protein was found to participate in signal transduction mediated by various growth factor receptors. CD47 has been demonstrated to be a ligand for this receptor protein. This gene and its product share very high similarity with several other members of the SIRP family. These related genes are located in close proximity to each other on chromosome 20p13. Multiple alternatively spliced transcript variants have been determined for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

SHPS1: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds FGR. Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB. Binds PTK2B. Ubiquitous. Highly expressed in brain. Detected on myeloid cells, but not T-cells. Detected at lower levels in heart, placenta, lung, testis, ovary, colon, liver, small intestine, prostate, spleen, kidney, skeletal muscle and pancreas. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Receptor, misc.; Cell adhesion; Membrane protein, integral; Cell surface; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 20p13

Cellular Component: membrane; plasma membrane; integral to membrane

Molecular Function: SH3 domain binding

Biological Process: cell adhesion; blood coagulation; leukocyte migration