Anti-SPAM1 Rabbit Monoclonal Antibody for WB, IHC-P, ELISA - P38567

Core Product Specifications and Parameters

Biological Background: SPAM1 Function and Localization

• SPAM1 (sperm adhesion molecule 1), also designated hyaluronidase PH-20, hyaluronoglucosaminidase PH-20, or sperm surface protein PH-20, is a glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein.
• It functions as a hyaluronidase, enzymatically digesting hyaluronic acid in the cumulus cell matrix surrounding the oocyte, thereby facilitating sperm penetration during fertilization.
• SPAM1 is critical for sperm-egg adhesion, mediating the initial contact between sperm and the cumulus-oocyte complex.
• As a member of the hyaluronidase family, it is classified as a glycosidase (hydrolase) specialized in hyaluronic acid degradation.
• The protein localizes to the sperm cell membrane and is expressed testis-specifically.
• Post‑translational modifications include N‑linked glycosylation, disulfide bond formation, and a GPI‑anchor that tethers it to the membrane.
• Alternative splicing yields multiple isoforms, potentially expanding its functional repertoire.

Experimental Guidance and Technical Tips

• The immunogen corresponds to an internal sequence (aa 61–223) of human SPAM1; therefore, the antibody is expected to recognize full-length SPAM1 and isoforms that include this region.
• For Western blot, consider using human testis lysate or sperm protein extract as a positive control, given the tissue‑specific expression; the predicted molecular weight is ~58 kDa, though glycosylation may cause a shift.
• In immunohistochemistry on paraffin‑embedded sections (IHC‑P), optimize antigen retrieval and validate reactivity in human testis tissue.
• For ELISA applications, utilize recombinant SPAM1 protein or cell lysates expressing the target for coating or detection.
• Cross‑reactivity with rat suggests epitope conservation; confirm suitability for rat samples via sequence alignment and experimental validation.

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