PRELP Protein, Human (HEK293, Fc)

The PRELP protein may be an anchoring factor that plays a crucial role in connecting the basement membrane and connective tissue, contributing to structural integrity. Its interaction with the heparan sulfate proteoglycan perlecan and type I and type II collagen emphasizes its versatile binding ability. PRELP Protein, Human (HEK293, Fc) is the recombinant human-derived PRELP protein, expressed by HEK293 , with N-mFc labeled tag.

PRELP Protein emerges as a potential anchoring factor linking basement membranes to the underlying connective tissue, suggesting a crucial role in structural integrity. This function implies its involvement in maintaining the stability and organization of extracellular matrices. PRELP specifically interacts with the basement membrane heparan sulfate proteoglycan perlecan and triple helical collagens type I and type II, underscoring its versatile binding capabilities and its significance in mediating molecular connections within the extracellular environment. The protein's dual ability to anchor to perlecan and collagens hints at its role in orchestrating the intricate composition of basement membranes, reflecting its potential contributions to tissue architecture and homeostasis. Further exploration of PRELP's interactions and functions may unveil its specific mechanisms in basement membrane anchoring and provide insights into its broader implications in connective tissue biology.

Human

HEK293

N-mFc

P51888 (Q21-I382)

5549  [NCBI]

Full Length of Mature Protein

QPTRRPRPGTGPGRRPRPRPRPTPSFPQPDEPAEPTDLPPPLPPGPPSIFPDCPRECYCPPDFPSALYCDSRNLRKVPVIPPRIHYLYLQNNFITELPVESFQNATGLRWINLDNNRIRKIDQRVLEKLPGLVFLYMEKNQLEEVPSALPRNLEQLRLSQNHISRIPPGVFSKLENLLLLDLQHNRLSDGVFKPDTFHGLKNLMQLNLAHNILRKMPPRVPTAIHQLYLDSNKIETIPNGYFKSFPNLAFIRLNYNKLTDRGLPKNSFNISNLLVLHLSHNRISSVPAINNRLEHLYLNNNSIEKINGTQICPNDLVAFHDFSSDLENVPHLRYLRLDGNYLKPPIPLDLMMCFRLLQSVVI

Approximately 80-90 kDa,based on SDS-PAGE under reducing conditions.

≥ 85%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.