SignalStar multiplex immunohistochemistry (IHC) is an advanced technology for labeling multiple proteins simultaneously in tissue samples using specific primary antibodies and fluorescent detection reagents. This technology offers accuracy and reliability in visualizing and analyzing protein expression while maintaining spatial context and tissue architecture.

SignalStar Oligo-Antibody Pairs are compatible with the SignalStar Multiplex IHC Buffer Kits for use in fluorescent multiplex imaging experiments. This product includes the oligo-conjugated antibodies and complementary oligos required for labeling your target protein on up to 10 slides. SignalStar Multiplex IHC Buffer Kits are required to amplify and image the target signal. Multiple oligo-antibody pairs can be conveniently combined into a multiplex panel using the SignalStar Multiplex IHC Panel Builder. SignalStar Multiplex IHC Kits & Reagents are not compatible with all of Cell Signaling Technology^® products and protocols that are recommended for use in immunohistochemical assays.

CD45 (D3F8Q) Rabbit mAb (SignalStar™ Conjugate 0046) recognizes endogenous levels of total CD45 protein. Non-specific staining was observed in mouse kidney by immunohistochemistry. This antibody is predicted to react with both the CD45.1 and CD45.2 alleles.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala1258 of mouse CD45 protein.

The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2,3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T- and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils, and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).