CD47 Human

CD47 Human Recombinant
Cat. No.
BT29820
Source
Sf9, Baculovirus cells.
Synonyms
CD47 Molecule, Antigenic Surface Determinant Protein OA3, CD47 Antigen (Rh-Related Antigen, Integrin-Associated Signal Transducer), Antigen Identified By Monoclonal Antibody 1D8, Integrin Associated Protein, Integrin-Associated Protein, Rh-Related Antigen, CD47 Glycoprotein, MER6, IAP, Integrin-Associated Signal Transducer, Leukocyte Surface Antigen CD47, CD47 Antigen, Protein MER6, OA3, CD47.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CD47 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-141 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 129 amino acids and having a molecular mass of 14.7kDa.
CD47 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Product Specs

Introduction
CD47, also known as integrin-associated protein (IAP), is a transmembrane receptor that interacts with several ligands, including thrombospondin-1 (THBS1) and signal regulatory protein alpha (SIRPα). CD47 plays diverse roles in cell adhesion, immune regulation, and neuronal function. As an adhesion receptor for THBS1 on platelets, CD47 participates in cell-cell interactions and platelet aggregation. It also modulates integrin activity, influencing cell migration and adhesion to the extracellular matrix. In the immune system, CD47 acts as a 'don't eat me' signal by binding to SIRPα on macrophages, thereby inhibiting phagocytosis and promoting self-tolerance. This interaction is crucial for preventing the premature destruction of red blood cells and maintaining immune homeostasis. Dysregulation of CD47-SIRPα signaling has been implicated in cancer immune evasion, making it a potential target for immunotherapy. Furthermore, CD47 contributes to memory formation and synaptic plasticity in the hippocampus, suggesting a role in cognitive function.
Description
Recombinant CD47 protein was expressed in Sf9 insect cells using a baculovirus expression system. The protein encompasses amino acids 19-141 of the human CD47 sequence, with a 6-amino acid Histidine tag added at the C-terminus for purification purposes. The resulting protein has a total of 129 amino acids and a molecular weight of 14.7 kDa. SDS-PAGE analysis under reducing conditions reveals multiple bands between 18-28 kDa, indicative of glycosylation. The protein was purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
Clear, colorless liquid, free from particulate matter
Formulation
The CD47 protein is supplied as a 1 mg/ml solution in phosphate-buffered saline (PBS) with a pH of 7.4 and 10% glycerol as a cryoprotectant.
Stability
For short-term storage (up to 4 weeks), the CD47 protein solution should be stored at 4°C. For long-term storage, it is recommended to freeze the protein at -20°C. Adding a carrier protein like bovine serum albumin (BSA) or human serum albumin (HSA) to a final concentration of 0.1% can help to stabilize the protein during freezing and thawing. Repeated freeze-thaw cycles should be avoided to prevent protein degradation.
Purity
The purity of the CD47 protein is greater than 95% as assessed by SDS-PAGE analysis.
Synonyms
CD47 Molecule, Antigenic Surface Determinant Protein OA3, CD47 Antigen (Rh-Related Antigen, Integrin-Associated Signal Transducer), Antigen Identified By Monoclonal Antibody 1D8, Integrin Associated Protein, Integrin-Associated Protein, Rh-Related Antigen, CD47 Glycoprotein, MER6, IAP, Integrin-Associated Signal Transducer, Leukocyte Surface Antigen CD47, CD47 Antigen, Protein MER6, OA3, CD47.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
QLLFNKTKSV EFTFCNDTVV IPCFVTNMEA QNTTEVYVKW KFKGRDIYTF DGALNKSTVP TDFSSAKIEV SQLLKGDASL KMDKSDAVSH TGNYTCEVTE LTREGETIIE LKYRVVSWFS PNEHHHHHH.

Product Science Overview

Structure and Expression

CD47 is a 47 kDa protein that appears at a position of 70 kDa upon SDS-PAGE due to its hyperglycosylated structure . It consists of:

  • An N-terminal extracellular IgV domain
  • Five transmembrane helices
  • A C-terminal cytoplasmic short variable spliced tail

There are four different spliced isoforms of CD47, with isoform 2 being the most abundantly expressed . CD47 is found on a variety of hematopoietic and non-hematopoietic cells, and its expression level varies depending on the cell type .

Function

CD47 is well-known for its immunoregulatory functions. It acts as a “don’t eat me” signal to prevent phagocytosis by macrophages . This receptor is crucial for maintaining immune system homeostasis by modulating cellular phagocytosis, transmigration of neutrophils, and activation of dendritic cells, T cells, and B cells .

In healthy cells, CD47 prevents phagocytosis, while aged and superfluous cells are removed through phagocytosis due to CD47 down-regulation . This regulatory function was first described in red blood cells but is now known to be widely expressed in other cell types as well .

Role in Cancer

CD47 is highly expressed in various types of cancer cells, allowing them to escape from the immune system . This makes CD47 a prominent target in cancer therapy. Blocking the interaction between CD47 and SIRPα can enhance cancer cell clearance by macrophages and increase antigen cross-presentation, leading to T-cell priming and an activated adaptive antitumor immune response .

Therapeutic Applications

Several strategies have been developed to target CD47 in cancer therapy, including:

  • Mimicry peptides
  • Antibodies
  • Gene silencing strategies

Among these, the use of anti-CD47 antibodies is the most advanced approach. These antibodies inhibit the CD47-SIRPα axis, enhancing cancer cell phagocytosis . Combining these antibodies with chemotherapy and immunotherapy has shown promise in improving the survival of cancer patients .

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