GLB1 Human
Sf9, Baculovirus cells.
lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 1
Greater than 90.0% as determined by SDS-PAGE.
Description
GLB1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 662 amino acids (24-677 a.a.) and having a molecular mass of 74.6 kDa.
GLB1 is fused to an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Beta-galactosidase, also known as GLB1, is a lysosomal enzyme responsible for hydrolyzing the terminal beta-galactose from ganglioside and keratin sulfate precursors. GLB1 plays a critical role in elastogenesis (the formation of extracellular elastic fibers) and connective tissue development. It exhibits similarities to elastin-binding protein, a crucial component of the non-integrin cell surface receptor. In elastin-secreting cells, GLB1 interacts intracellularly with tropoelastin, functioning as a recycling molecular chaperone.
Recombinant human GLB1, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It comprises 662 amino acids (with a sequence spanning from amino acid 24 to 677) and has a molecular weight of 74.6 kDa.
For purification and detection purposes, the GLB1 protein contains an 8-amino acid Histidine tag fused at its C-terminus. The protein has been purified using proprietary chromatographic methods.
The GLB1 human protein solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
To further enhance stability during prolonged storage, consider adding a carrier protein (such as HSA or BSA) to a final concentration of 0.1%.
Repeated freezing and thawing of the protein solution should be avoided.
The purity of the GLB1 protein is greater than 90.0%, as determined by SDS-PAGE analysis.
lacZ, beta-gal, b-gal, Acid beta-galactosidase, Lactase, Elastin receptor 1
Sf9, Baculovirus cells.
LRNATQRMFE IDYSRDSFLK DGQPFRYISG SIHYSRVPRF YWKDRLLKMK MAGLNAIQTY VPWNFHEPWP GQYQFSEDHD VEYFLRLAHE LGLLVILRPG PYICAEWEMG GLPAWLLEKE SILLRSSDPD YLAAVDKWLG VLLPKMKPLL YQNGGPVITV QVENEYGSYF ACDFDYLRFL QKRFRHHLGD DVVLFTTDGA HKTFLKCGAL QGLYTTVDFG TGSNITDAFL SQRKCEPKGP LINSEFYTGW LDHWGQPHST IKTEAVASSL YDILARGASV NLYMFIGGTN FAYWNGANSP YAAQPTSYDY DAPLSEAGDL TEKYFALRNI IQKFEKVPEG PIPPSTPKFA YGKVTLEKLK TVGAALDILC PSGPIKSLYP LTFIQVKQHY GFVLYRTTLP QDCSNPAPLS SPLNGVHDRA YVAVDGIPQG VLERNNVITL NITGKAGATL DLLVENMGRV NYGAYINDFK GLVSNLTLSS NILTDWTIFP LDTEDAVRSH LGGWGHRDSG HHDEAWAHNS SNYTLPAFYM GNFSIPSGIP DLPQDTFIQF PGWTKGQVWI NGFNLGRYWP ARGPQLTLFV PQHILMTSAP NTITVLELEW APCSSDDPEL CAVTFVDRPV IGSSVTYDHP SKPVEKRLMP PPPQKNKDSW LDHVLEHHHH HH
Product Science Overview
The gene encoding GLB1 is located on chromosome 3p22.3 . Mutations in this gene can lead to lysosomal storage diseases such as GM1-gangliosidosis and Morquio B syndrome (mucopolysaccharidosis IVB) . These conditions are characterized by the accumulation of undigested substrates within the lysosomes, leading to cellular dysfunction and various clinical manifestations.
Recombinant human beta-galactosidase-1 (rhGLB1) is produced using Chinese Hamster Ovary (CHO) cells . The recombinant form is designed to mimic the natural enzyme’s activity and is used in various research and therapeutic applications. The recombinant protein is typically tagged with a C-terminal 6-His tag for purification purposes .
- Research: rhGLB1 is widely used in biochemical and cell biology research to study lysosomal function and the pathogenesis of lysosomal storage diseases .
- Therapeutics: Recombinant enzymes are being explored as potential treatments for lysosomal storage diseases through enzyme replacement therapy (ERT). By supplementing the deficient enzyme, ERT aims to reduce the accumulation of substrates and alleviate disease symptoms .
The production of rhGLB1 involves the expression of the human GLB1 gene in CHO cells. The recombinant protein is then purified using affinity chromatography, leveraging the 6-His tag for efficient isolation . The purified enzyme is characterized by its ability to cleave specific substrates, such as 4-Methylumbelliferyl-beta-D-galactopyranoside, with high specificity and activity .
Deficiencies in GLB1 activity can lead to severe clinical conditions. GM1-gangliosidosis presents with neurological deterioration, skeletal abnormalities, and organomegaly, while Morquio B syndrome primarily affects skeletal development . Early diagnosis and potential treatments, including ERT, are critical for managing these conditions.
