Recombinant Human Hyaluronidase PH-20 | MyBioSource MBS963588 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Hyaluronidase PH-20

catalog :

MBS963588

quantity :

0.05 mg (E-Coli)

price :

185 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS963588

products type :

Recombinant Protein

products full name :

Recombinant Human Hyaluronidase PH-20

products short name :

Hyaluronidase PH-20

products name syn :

Hyaluronoglucosaminidase PH-20; Sperm adhesion molecule 1; Sperm surface protein PH-20

other names :

hyaluronidase PH-20 isoform 2; Hyaluronidase PH-20; hyaluronidase PH-20; sperm adhesion molecule 1 (PH-20 hyaluronidase, zona pellucida binding); Hyaluronoglucosaminidase PH-20; Sperm adhesion molecule 1; Sperm surface protein PH-20

products gene name :

SPAM1

other gene names :

SPAM1; SPAM1; HYA1; PH20; HYAL1; HYAL3; HYAL5; PH-20; SPAG15; HEL-S-96n; HYAL3; PH20; Hyal-PH20

uniprot entry name :

HYALP_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

36-490

sequence length :

509

sequence :

LNFRAPPVIPNVPFLWAWNAPSEFCLGKFDEPLDMSLFS
FIGSPRINATGQGVTIFYVDRLGYYPYIDSITGVTVNGG
IPQKISLQDHLDKAKKDITFYMPVDNLGMAVIDWEEWRP
TWARNWKPKDVYKNRSIELVQQQNVQLSLTEATEKAKQE
FEKAGKDFLVETIKLGKLLRPNHLWGYYLFPDCYNHHYK
KPGYNGSCFNVEIKRNDDLSWLWNESTALYPSIYLNTQQ
SPVAATLYVRNRVREAIRVSK

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Cancer

products description :

Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are bedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.

products references :

Molecular cloning of the human and monkey sperm surface protein PH-20.Lin Y., Kimmel L.H., Myles D.G., Primakoff P.Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993) The human sperm protein PH-20 has hyaluronidase activity.Gmachl M., Sagan S., Ketter S., Kreil G.FEBS Lett. 336:545-548(1993) Expression analysis, genomic structure, and mapping to 7q31 of the human sperm adhesion molecule gene SPAM1.Jones M.H., Davey P.M., Aplin H., Affara N.A.Genomics 29:796-800(1995) The DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003) Human chromosome 7 DNA sequence and biology.Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.Science 300:767-772(2003) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. In vitro mutagenesis of PH-20 hyaluronidase from human sperm.Arming S., Strobl B., Wechselberger C., Kreil G.Eur. J. Biochem. 247:810-814(1997) Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma.Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.Nature 469:539-542(2011)

ncbi gi num :

291290979

ncbi acc num :

NP_001167515.1

ncbi gb acc num :

NM_001174044.1

uniprot acc num :

P38567

ncbi mol weight :

67.83kD

ncbi pathways :

Chondroitin Sulfate Degradation Pathway (413376); Chondroitin Sulfate Degradation Pathway (468247); Dermatan Sulfate Degradation Pathway (413375); Dermatan Sulfate Degradation Pathway (468240); Fertilization Pathway (1269334); Glycosaminoglycan Degradation Pathway (82981); Glycosaminoglycan Degradation Pathway (355); Interaction With Cumulus Cells Pathway (1269336); Metabolic Pathways (132956); Reproduction Pathway (1269333)

ncbi summary :

Hyaluronidase degrades hyaluronic acid, a major structural proteoglycan found in extracellular matrices and basement membranes. Six members of the hyaluronidase family are clustered into two tightly linked groups on chromosome 3p21.3 and 7q31.3. This gene was previously referred to as HYAL1 and HYA1 and has since been assigned the official symbol SPAM1; another family member on chromosome 3p21.3 has been assigned HYAL1. This gene encodes a GPI-anchored enzyme located on the human sperm surface and inner acrosomal membrane. This multifunctional protein is a hyaluronidase that enables sperm to penetrate through the hyaluronic acid-rich cumulus cell layer surrounding the oocyte, a receptor that plays a role in hyaluronic acid induced cell signaling, and a receptor that is involved in sperm-zona pellucida adhesion. Abnormal expression of this gene in tumors has implicated this protein in degradation of basement membranes leading to tumor invasion and metastasis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010]

uniprot summary :

SPAM1: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid. Belongs to the glycosyl hydrolase 56 family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: EC 3.2.1.35; Hydrolase; Glycan Metabolism - glycosaminoglycan degradation; Membrane protein, GPI anchor; Cell surface. Chromosomal Location of Human Ortholog: 7q31.3. Cellular Component: plasma membrane. Molecular Function: hyalurononglucosaminidase activity. Biological Process: binding of sperm to zona pellucida; carbohydrate metabolic process; cell adhesion; fusion of sperm to egg plasma membrane; multicellular organism reproduction; single fertilization; sperm-egg recognition

size1 :

0.05 mg (E-Coli)

price1 :

185 USD

size2 :

0.2 mg (E-Coli)

price2 :

420

size3 :

0.5 mg (E-Coli)

price3 :

680

size4 :

1 mg (E-Coli)

price4 :

1070

more info or order :

MyBioSource product webpage