SPAM1抗体—艾普蒂

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     Western blot analysis of Keratin 18 in Hela, K562 lysates using Cytokeratin 18 antibody.    

  
  

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     Immunocytochemistry analysis of Cytokeratin 18(green) in Hela using Cytokeratin 18 antibody,and DAPI(blue)    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human Cholangiocarcinoma using Cytokeratin 18 antibody. High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

The SPAM1 (Sperm Adhesion Molecule 1) antibody targets the SPAM1 protein, also known as PH-20. a glycosylphosphatidylinositol (GPI)-anchored membrane protein primarily associated with sperm function. Discovered in the 1980s, SPAM1/PH-20 is expressed in the testis and localizes to the sperm's acrosomal membrane and plasma membrane. It exhibits hyaluronidase activity, critical for sperm penetration through the hyaluronic acid-rich extracellular matrix of the oocyte during fertilization. This dual enzymatic and adhesion role makes SPAM1 essential for reproductive biology.

SPAM1 antibodies are widely used in research to study sperm maturation, fertilization mechanisms, and infertility. They help detect SPAM1 expression patterns, assess its enzymatic function, and explore its role in pathologies like male infertility or certain cancers where SPAM1 is aberrantly expressed. Monoclonal and polyclonal antibodies against SPAM1 have also been investigated for contraceptive development, aiming to block its hyaluronidase activity or sperm-egg binding.

Additionally, SPAM1's homology with HYAL5 and its presence in somatic tissues (e.g., some tumors) have spurred interest in its oncogenic potential. Antibodies here aid in elucidating SPAM1's involvement in cancer metastasis via hyaluronan degradation. Overall, SPAM1 antibodies serve as vital tools in reproductive health, cancer research, and therapeutic innovation.