SIRP Beta 1 Protein, Human (Biotinylated, HEK293, C-His-Avi)

SIRP beta 1 protein negatively regulates receptor tyrosine kinase signaling and recruits SYK for myeloid cell activation. It interacts with TYROBP as a homodimer, facilitating SYK recruitment. This intricate molecular interplay is crucial for modulating myeloid cell activation and regulating cellular signaling. SIRP beta 1 occupies a central position in protein interactions that contribute to its functional role. SIRP Beta 1 Protein, Human (Biotinylated, HEK293, C-His-Avi) is the recombinant human-derived SIRP Beta 1 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of SIRP Beta 1 Protein, Human (Biotinylated, HEK293, C-His-Avi) is 340 a.a., with molecular weight of 55-65 kDa.

SIRP beta 1 protein, an immunoglobulin-like cell surface receptor, plays a vital role in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Additionally, it participates in the recruitment of the tyrosine kinase SYK, triggering the activation of myeloid cells when associated with TYROBP. Existing as a homodimer with disulfide linkages, SIRP beta 1 interacts specifically with TYROBP, leading to the recruitment of SYK. This intricate molecular interplay positions SIRP beta 1 at the nexus of cellular signaling regulation, highlighting its significance in modulating myeloid cell activation and the intricate network of protein interactions that contribute to its functional role.

Human

HEK293

C-Avi;C-His

O00241-1 (E30-A369)

10326  [NCBI]

55-65 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.