CENPB Protein, Human (sf9, His)

CENPB proteins form antiparallel homodimers, interact with centromeric heterochromatin, and specifically bind to the CENP-B box (a 17 bp subset of α-class satellite DNA). This interaction is critical for organizing centromeric satellite DNA into higher-order structures, promoting centromere assembly, and directing centromere formation in mammalian chromosomes. CENPB Protein, Human (sf9, His) is the recombinant human-derived CENPB protein, expressed by Sf9 insect cells , with N-His labeled tag.

The CENPB protein plays a pivotal role in centromere organization by interacting with centromeric heterochromatin in chromosomes and binding specifically to a 17 bp subset of alphoid satellite DNA known as the CENP-B box. This interaction is crucial for the potential organization of centromere satellite DNA into a higher-order structure, likely directing centromere formation and facilitating kinetochore assembly in mammalian chromosomes. CENPB forms an antiparallel homodimer and also interacts with CENPT. Furthermore, it has been identified as a component of a centromere complex that includes histones H2A, H2B, and H4, along with at least CENPA, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1, and RSF1, underscoring its integral role in the intricate architecture of the centromeric region.

Human

Sf9 insect cells

N-10*His

P07199 (M1-S599)

1059  [NCBI]

Full Length

MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLTEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTSLKSEGEEEEEEEEEEEEEEGEGEEEEEEGEEEEEEGGEGEELGEEEEVEEEGDVDSDEEEEEDEESSSEGLEAEDWAQGVVEAGGSFGAYGAQEEAQCPTLHFLEGGEDSDSDSEEEDDEEEDDEDEDDDDDEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS

Approximately 78-85 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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  ≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.