SPAM1 Antibody (D-9): sc-518256

SPAM1 Antibody (D-9) is a mouse monoclonal IgG1 kappa light chain antibody that binds to an epitope mapping between amino acids 144-166 of the human SPAM1 protein. SPAM1, also known as Sperm Adhesion Molecule 1 or hyaluronidase PH-20, is a glycosylphosphatidylinositol (GPI)-anchored enzyme predominantly localized on the plasma membrane and inner acrosomal membrane of sperm cells, where SPAM1 plays a crucial role in fertilization. As a member of the hyaluronidase family, SPAM1 exhibits hyaluronidase activity that hydrolyzes hyaluronic acid (HA), a major glycosaminoglycan component of the extracellular matrix and the cumulus oophorus surrounding the oocyte. By degrading HA, SPAM1 facilitates sperm penetration through the HA-rich cumulus cell layer, enabling access to the oocyte. This process is essential for sperm motility and successful sperm-egg interaction, including initial adhesion and binding to the zona pellucida. SPAM1 functions in coordination with other sperm surface proteins such as acrosin and IZUMO1, which are critical for the acrosome reaction and membrane fusion with the oocyte. These interactions collectively enable sperm to overcome structural barriers and achieve fertilization. Beyond reproduction, SPAM1′s ability to degrade HA may also have implications in cellular signaling and tissue remodeling processes. Anti-SPAM1 antibody (D-9) is reactive with human samples and has been validated for use in western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Available in both non-conjugated and conjugated forms, including horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and various Alexa Fluor® conjugates, SPAM1 (D-9) antibody offers versatility for a wide range of experimental needs.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

SPAM1 Antibody (D-9) References:

1. Mouse Spam1 (PH-20) is a multifunctional protein: evidence for its expression in the female reproductive tract.  |  Zhang, H. and Martin-DeLeon, PA. 2003. Biol Reprod. 69: 446-54. PMID: 12672666
2. SPAM1 (PH-20) protein and mRNA expression in the epididymides of humans and macaques: utilizing laser microdissection/RT-PCR.  |  Evans, EA., et al. 2003. Reprod Biol Endocrinol. 1: 54. PMID: 12932297
3. Transcription of the human and rodent SPAM1 / PH-20 genes initiates within an ancient endogenous retrovirus.  |  Dunn, CA. and Mager, DL. 2005. BMC Genomics. 6: 47. PMID: 15804358
4. Spam1-associated transmission ratio distortion in mice: elucidating the mechanism.  |  Martin-DeLeon, PA., et al. 2005. Reprod Biol Endocrinol. 3: 32. PMID: 16092963
5. Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis.  |  Jedrzejas, MJ. and Stern, R. 2005. Proteins. 61: 227-38. PMID: 16104017
6. Differential selectivity of hyaluronidase inhibitors toward acidic and basic hyaluronidases.  |  Isoyama, T., et al. 2006. Glycobiology. 16: 11-21. PMID: 16166602
7. Epididymal SPAM1 and its impact on sperm function.  |  Martin-DeLeon, PA. 2006. Mol Cell Endocrinol. 250: 114-21. PMID: 16420970
8. cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals.  |  Lathrop, WF., et al. 1990. J Cell Biol. 111: 2939-49. PMID: 2269661
9. A hyaluronidase activity of the sperm plasma membrane protein PH-20 enables sperm to penetrate the cumulus cell layer surrounding the egg.  |  Lin, Y., et al. 1994. J Cell Biol. 125: 1157-63. PMID: 8195297
10. Molecular cloning of the human and monkey sperm surface protein PH-20.  |  Lin, Y., et al. 1993. Proc Natl Acad Sci U S A. 90: 10071-5. PMID: 8234258
11. The human sperm protein PH-20 has hyaluronidase activity.  |  Gmachl, M., et al. 1993. FEBS Lett. 336: 545-8. PMID: 8282124
12. Expression analysis, genomic structure, and mapping to 7q31 of the human sperm adhesion molecule gene SPAM1.  |  Jones, MH., et al. 1995. Genomics. 29: 796-800. PMID: 8575780

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-SPAM1 Antibody (D-9) has 0 citations in a variety of scientific publications.

Primary antibodies like Anti-SPAM1 Antibody (D-9) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

SPAM1 Antibody (D-9) Specifications

Alternate Product Name: SPAM1

Product Clone Name: D-9

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG₁ kappa light chain

Amino Acids: 144-166

Epitope Target: SPAM1

Epitope Species: human

Product Reactivity/Detection: SPAM1

Species Reactivity/Detection: human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, ELISA

Vialing Information: Each vial contains 200 µg IgG₁ kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 0 citations in various scientific publications

Available Conjugates/Forms for SPAM1 Antibody (D-9): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin