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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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CD5 (CD5 molecule) is a type I transmembrane glycoprotein of the scavenger receptor cysteine-rich (SRCR) superfamily, expressed on the surface of T lymphocytes and a subset of B cells where it participates in immune signaling and cell-cell interaction. CD5 Antibody N-Terminus / CD5 N-Terminal Antibody (clone RM354) is designed to detect the extracellular N-terminal region of CD5, enabling targeted analysis of the surface-exposed domain responsible for ligand interaction and immune cell communication. CD5 antibody, also known as T cell surface glycoprotein CD5 antibody or LEU1 antibody, is widely used in studies of immune cell surface markers and lymphocyte identification, with N-terminal targeting providing optimal access to extracellular epitopes.
The N-terminal region of CD5 forms part of its extracellular domain, which consists of SRCR motifs involved in ligand binding and interaction with other immune components. This region is accessible on the cell surface, making CD5 N-terminal antibody particularly well suited for detecting CD5 in intact cells without the need for permeabilization. As a result, CD5 N-terminus antibody is highly relevant for applications focused on cell surface expression, immune cell phenotyping, and extracellular signaling analysis.
Detection of the CD5 N-terminus enables detailed analysis of surface expression patterns across lymphocyte populations, supporting studies of immune cell distribution, tissue localization, and cellular interaction within lymphoid organs. CD5 antibody targeting the N-terminal domain is especially useful for identifying T cell populations in tissue sections and cell-based assays where preservation of membrane integrity is important.
The extracellular domain of CD5 is also involved in modulating immune responses through interactions at the cell surface, including participation in signaling complexes at the immunological synapse. CD5 N-terminal antibody supports investigation of these processes by enabling detection of the ligand-interacting region of the protein, providing insight into how CD5 contributes to immune communication and signal initiation.
In addition, targeting the N-terminal region ensures detection of full-length, membrane-associated CD5 in its native conformation. This makes CD5 N-terminus antibody particularly valuable for studies focused on receptor biology, cell surface accessibility, and immune cell classification. Its specificity for the extracellular domain allows for accurate identification of CD5-positive cells in both tissue and suspension-based assays.
This recombinant rabbit monoclonal antibody clone RM354 provides consistent recognition of the CD5 N-terminal region and supports reliable detection in research applications focused on surface expression and immune cell identification. Its epitope-specific targeting enhances experimental precision in studies requiring accurate detection of extracellular CD5.
Because the N-terminal domain of CD5 is essential for cell surface expression and immune interaction, CD5 N-terminal antibody is widely used in studies of lymphocyte identification, immune cell communication, extracellular signaling, and surface marker analysis.
A full range of CD5 antibody reagents for immunohistochemistry, western blot, and flow cytometry is available on our CD5 Antibody collection page.
The stated application concentrations are suggested starting points. Titration of the CD5 Antibody N-Terminus / CD5 N-Terminal Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A peptide corresponding to the N-terminus (extracellular domain) of human T-cell surface glycoprotein CD5 was used as the immunogen for the CD5 antibody.
Store the recombinant CD5 antibody at -20oC.
CD5 N-terminal antibody, CD5 N terminus antibody, CD5 extracellular domain antibody, CD5 surface epitope antibody, CD5 N terminal epitope antibody
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