HEXB/Hexosaminidase B Protein, Human (HEK293, His)
HEXB (hexosaminidase B) proteolytically hydrolyzes N-acetyl-D-hexosamine and/or sulfated residues in glycoconjugates, including oligosaccharides, glycolipids, and mucopolysaccharides. B isoenzymes efficiently hydrolyze neutral oligosaccharides, making them unique. HEXB/Hexosaminidase B Protein, Human (HEK293, His) is the recombinant human-derived HEXB/Hexosaminidase B protein, expressed by HEK293 , with C-His labeled tag.
- Species: Human
- Source: HEK293
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Storage:Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Biological Activity
Description
HEXB (hexosaminidase B) proteolytically hydrolyzes N-acetyl-D-hexosamine and/or sulfated residues in glycoconjugates, including oligosaccharides, glycolipids, and mucopolysaccharides. B isoenzymes efficiently hydrolyze neutral oligosaccharides, making them unique. HEXB/Hexosaminidase B Protein, Human (HEK293, His) is the recombinant human-derived HEXB/Hexosaminidase B protein, expressed by HEK293 , with C-His labeled tag.
Background
HEXB (Hexosaminidase B) protein exhibits hydrolytic activity towards the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine residues found in various glycoconjugates, including oligosaccharide moieties from proteins, neutral glycolipids, and specific mucopolysaccharides. Notably, the B isozyme demonstrates efficient hydrolysis of neutral oligosaccharides, distinguishing it from other substrates. While isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A, isozyme B does not participate in this process. During fertilization, HEXB, specifically isozyme B, plays a crucial role in the zona block to polyspermy. It is localized in the cortical granules of non-activated oocytes and is exocytosed during the cortical reaction triggered by oocyte activation. This exocytosis results in the inactivation of the sperm galactosyltransferase-binding site, contributing to the prevention of sperm binding to the zona pellucida and ensuring the integrity of the zona block to polyspermy.
MCE Validation Data
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Purity - SDS-PAGE
Purity - SDS-PAGE
Technical Parameters
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Species Human
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Source HEK293
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Tag C-His
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Accession
P07686 (A43-M556)
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Molecular Construction
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N-term
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HEXB (A43-M556)
Accession # P07686 -
His
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C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
HEXB; HEL-248; Hexosaminidase Subunit Beta; HCC-7; Beta-Hexosaminidase Subunit Beta; Epididymis Secretory Sperm Binding Protein; N-Acetyl-Beta-Glucosaminidase Subunit Beta; Epididymis Secretory Protein Li 111; Beta-N-Acetylhexosaminidase Subunit Beta; Bet
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AA Sequence
ARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM
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Predicted Molecular Mass
60.2 kDa
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Molecular Weight
Approximately 60-66 kDa, based on SDS-PAGE under reducing conditions.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Solution
<1 EU/μg, determined by LAL method.
Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Shipping with dry ice.
Documentation
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Data Sheet (238 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)