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Human SPAM1 (PH-20) Recombinant

SPAM1

accession:  P38567
   Size A     5ug   $ 160
   Size B      25ug  $680
   Size C      100ug  $ 1950
Domain  : 
Gene  :  SPAM1
Catalog no. :  RKP38567

 

Source:

Optimized DNA sequence  encoding extracellular domain of human  SPAM1 (PH20)  (LEU36 - TYR482) including a C-terminal His tag was expressed in HEK293 cells.


 
Molecular weight:

Recombinant human SPAM1 (PH20) is a protein consisting of 452 amino acid residue subunits,due to glycosylation migrates as an approximately as 64kDa band protein on reduced SDS-PAGE.


 
Purity:
>95%, as determined by SDS-PAGE and HPLC
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Human SPAM-1 (PH-20)  is lyophilized  from 0.2 μm filtered PBS solution, pH7.2 ,  5% Trehalose.

              
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

 
Storage:
Recombinant SPAM-1 (PH-20)  can be stored in working aliquots at 2° - 8° C for one month, or at -20°C to -70°C for twelve months.

Avoid repeated freeze/thaw cycles.

 
Usage:
This product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

PH-20

PH-20 is a glycosyl phosphatidylinositol (GPI)- linked sperm surface protein with hyaluronidase and zona- binding activity. The sperm adhesion molecule 1 (SPAM1 or PH-20) is an important sperm surface protein with bifunctional roles in mammalian fertilization. It has a hyaluronidase activity that is necessary for sperm to penetrate the cumulus cells surrounding the egg.

Related Publications:
kinetics of hyal-1 and PH-20 hyaluronidases: comparison of minimal substrates and analysis of the transglycosylation reaction
Glycobiology, Sep 2007; 17: 963 - 971.
spam1 (PH-20) expression in the extratesticular duct and accessory organs of the mouse: a possible role in sperm fluid reabsorption
Biol Reprod, Oct 2004; 71: 1101 - 1107.
mouse spam1 (PH-20) is a multifunctional protein: evidence for its expression in the female reproductive tract
Biol Reprod, Aug 2003; 69: 446 - 454.
mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg
J. Biol. Chem., Aug 2002; 277: 30310 - 30314.
posttranslational processing of PH-20 during epididymal sperm maturation in the horse
Biol Reprod, Nov 2001; 65: 1324 - 1331.




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by species:
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Antibodies:
Purified Polyclonal
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product_icon_8.jpg Human SPAM1 (PH-20) Recombinant
 
 
 
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