LYPD3/C4.4A 蛋白, Mouse (HEK293, His)

The LYPD3/C4.4A protein is a multifunctional cell surface molecule that is critical for cell migration and has been implicated in potential tumor progression. It binds laminin 1 and laminin 5, emphasizing its role in extracellular matrix interactions. LYPD3/C4.4A Protein, Mouse (HEK293, His) is the recombinant mouse-derived LYPD3/C4.4A protein, expressed by HEK293 , with C-His labeled tag.

LYPD3/C4.4A 蛋白是一种多功能细胞表面分子，在支持细胞迁移中发挥着至关重要的作用，并与肿瘤进展的潜在贡献有关。该蛋白对层粘连蛋白 1 和层粘连蛋白 5 表现出结合亲和力，突出显示其参与与细胞外基质成分的相互作用。此外，LYPD3/C4.4A 与 LGALS3 相互作用，表明其在受半乳糖凝集素相互作用影响的细胞过程中发挥作用。此外，它与 AGR2 和 AGR3 的关联意味着可能参与与肿瘤发生和进展相关的途径。LYPD3/C4.4A 的多方面相互作用强调了其在细胞动力学中的重要性及其对病理过程的潜在影响，特别是在肿瘤生物学背景下。

Measured by its binding ability in a functional ELISA. When LYPD3 is immobilized at 0.5 μg/mL (100 μL/well), Galectin-3 binds with an apparent KD is 109.3nM.

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  Measured by its binding ability in a functional ELISA. When LYPD3 is immobilized at 0.5 μg/mL (100 μL/well), Galectin-3 binds with an apparent KD is 109.3 nM.

Mouse

HEK293

C-His

Q91YK8 (L33-H287)

72434  [NCBI]

LECYSCVQKADDGCSPHRMKTVKCGPGVDVCTEAVGAVETIHGQFSVAVRGCGSGIPGKNDRGLDLHGLLAFFQLQQCSEDRCNAKLNLTLRGLNPAGNESAYEPNGAECYSCVGLSREKCQGSMPPVVNCYNASGRVYKGCFDGNVTLTAANVTVSLPVRGCVQDETCTRDGVTGPGFTLSGSCCQGPRCNADLRNKTYFSPRIPPLVLLPPPTTAAPSTRAQNSSSTTSTAAPTTTTSIIKPTTAQASHTSPH

The protein migrates as approximately 45-75 kDa under reducing SDS-PAGE due to glycosylation.

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

无菌粉末

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.