HEK293 Cells.
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
Greater than 95% as determined by SDS-PAGE.
SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.
SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Signal-Regulatory Protein Alpha (SIRPA) is a member of the signal-regulatory-protein (SIRP) family, which belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins involved in the negative regulation of receptor tyrosine kinase-coupled signaling.
SIRPA is subject to phosphorylation by tyrosine kinases. Its phosphorylated tyrosine residues recruit SH2 domain-containing tyrosine phosphatases (PTPs) and act as PTP substrates. SIRPA plays a role in signal transduction pathways mediated by various growth factor receptors. CD47 has been identified as a ligand for SIRPA.
Recombinant Human SIRPA, expressed in HEK293 cells, is a single, glycosylated polypeptide chain encompassing amino acids 27-373. With a molecular weight of 39kDa, this protein comprises 356 amino acids.
A 6-amino acid His-tag is fused to the C-terminus of SIRPA, facilitating purification via proprietary chromatographic methods.
The SIRPA solution is provided at a concentration of 1mg/ml in Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, freezing at -20°C is recommended.
Adding a carrier protein (0.1% HSA or BSA) is advised for long-term storage.
Repeated freeze-thaw cycles should be avoided.
Purity exceeds 95% as determined by SDS-PAGE analysis.
The protein's biological activity is assessed through its binding affinity to Human CD47 in a functional ELISA.
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
HEK293 Cells.
DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY HHHHHH.
Signal-Regulatory Protein Alpha (SIRPα) is a regulatory membrane glycoprotein that belongs to the SIRP family. It is primarily expressed by myeloid cells, stem cells, and neurons. SIRPα plays a crucial role in the immune system by acting as an inhibitory receptor and interacting with CD47, a transmembrane protein also known as the “don’t eat me” signal .
SIRPα is a single, glycosylated polypeptide chain that contains 356 amino acids and has a molecular mass of approximately 39 kDa. The recombinant form of SIRPα, produced in HEK293 cells, is often fused to a 6 amino acid His-tag at the C-terminus for purification purposes . The protein is expressed in various tissues, including the right frontal lobe, cerebellum, thalamus, prefrontal cortex, and amygdala .
SIRPα is involved in several biological processes, including:
The recombinant form of SIRPα is produced in HEK293 cells, a human embryonic kidney cell line. This expression system is chosen for its ability to produce high yields of glycosylated proteins that are biologically active. The recombinant protein is purified using proprietary chromatographic techniques to achieve high purity levels (>95%) and low endotoxin levels (<1 EU/µg) .
Recombinant SIRPα is used in various research applications, including: