Recombinant Full Length Human AGL Protein, C-Flag-tagged
Cat.No. : | AGL-44HFL |
Product Overview : | Recombinant Full Length Human AGL Protein, fused to Flag-tag at C-terminus, was expressed in Mammalian cells. |
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Description : | This gene encodes the glycogen debrancher enzyme which is involved in glycogen degradation. This enzyme has two independent catalytic activities which occur at different sites on the protein: a 4-alpha-glucotransferase activity and a amylo-1,6-glucosidase activity. Mutations in this gene are associated with glycogen storage disease although a wide range of enzymatic and clinical variability occurs which may be due to tissue-specific alternative splicing. Alternatively spliced transcripts encoding different isoforms have been described. |
Source : | Mammalian cells |
Species : | Human |
Tag : | Flag |
Form : | 25 mM Tris HCl, pH 7.3, 100 mM glycine, 10% glycerol. |
Molecular Mass : | 174.6 kDa |
AA Sequence : | MGHSKQIRILLLNEMEKLEKTLFRL EQGYELQFRLGPTLQGKAVTVYTNY PFPGETFNREKFRSLDWENP TEREDDSDKYCKLNLQQSGSFQYYF LQGNEKSGGGYIVVDPILRVGADNH VLPLDCVTLQTFLAKCLGPF DEWESRLRVAKESGYNMIHFTPLQT LGLSRSCYSLANQLELNPDFSRPNR KYTWNDVGQLVEKLKKEWNV ICITDVVYNHTAANSKWIQEHPECA YNLVNSPHLKPAWVLDRALWRFSCD VAEGKYKEKGIPALIENDHH MNSIRKIIWEDIFPKLKLWEFFQVD VNKAVEQFRRLLTQENRRVTKSDPN QHLTIIQDPEYRRFGCTVDM NIALTTFIPHDKGPAAIEECCNWFH KRMEELNSEKHRLINYHQEQAVNCL LGNVFYERLAGHGPKLGPVT RKHPLVTRYFTFPFEEIDFSMEESM IHLPNKACFLMAHNGWVMGDDPLRN FAEPGSEVYLRRELICWGDS VKLRYGNKPEDCPYLWAHMKKYTEI TATYFQGVRLDNCHSTPLHVAEYML DAARNLQPNLYVVAELFTGS EDLDNVFVTRLGISSLIREAMSAYN SHEEGRLVYRYGGEPVGSFVQPCLR PLMPAIAHALFMDITHDNEC PIVHRSAYDALPSTTIVSMACCASG STRGYDELVPHQISVVSEERFYTKW NPEALPSNTGEVNFQSGIIA ARCAISKLHQELGAKGFIQVYVDQV DEDIVAVTRHSPSIHQSVVAVSRTA FRNPKTSFYSKEVPQMCIPG KIEEVVLEARTIERNTKPYRKDENS INGTPDITVEIREHIQLNESKIVKQ AGVATKGPNEYIQEIEFENL SPGSVIIFRVSLDPHAQVAVGILRN HLTQFSPHFKSGSLAVDNADPILKI PFASLASRLTLAELNQILYR CESEEKEDGGGCYDIPNWSALKYAG LQGLMSVLAEIRPKNDLGHPFCNNL RSGDWMIDYVSNRLISRSGT IAEVGKWLQAMFFYLKQIPRYLIPC YFDAILIGAYTTLLDTAWKQMSSFV QNGSTFVKHLSLGSVQLCGV GKFPSLPILSPALMDVPYRLNEITK EKEQCCVSLAAGLPHFSSGIFRCWG RDTFIALRGILLITGRYVEA RNIILAFAGTLRHGLIPNLLGEGIY ARYNCRDAVWWWLQCIQDYCKMVPN GLDILKCPVSRMYPTDDSAP LPAGTLDQPLFEVIQEAMQKHMQGI QFRERNAGPQIDRNMKDEGFNITAG VDEETGFVYGGNRFNCGTWM DKMGESDRARNRGIPATPRDGSAVE IVGLSKSAVRWLLELSKKNIFPYHE VTVKRHGKAIKVSYDEWNRK IQDNFEKLFHVSEDPSDLNEKHPNL VHKRGIYKDSYGASSPWCDYQLRPN FTIAMVVAPELFTTEKAWKA LEIAEKKLLGPLGMKTLDPDDMVYC GIYDNALDNDNYNLAKGFNYHQGPE WLWPIGYFLRAKLYFSRLMG PETTAKTIVLVKNVLSRHYVHLERS PWKGLPELTNENAQYCPFSCETQAW SIATILETLYDLTRTRPLEQKLISE EDLAANDILDYKDDDDKV |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining. |
Stability : | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : | Store at -80 centigrade. |
Concentration : | >50 ug/mL as determined by microplate BCA method. |
Preparation : | Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. |
Protein Families : | Druggable Genome |
Protein Pathways : | Metabolic pathways, Starch and sucrose metabolism |
Gene Name : | AGL amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase [ Homo sapiens (human) ] |
Official Symbol : | AGL |
Synonyms : | GDE |
Gene ID : | 178 |
mRNA Refseq : | NM_000642.3 |
Protein Refseq : | NP_000633.2 |
MIM : | 610860 |
UniProt ID : | P35573 |
Products Types
◆ Recombinant Protein | ||
AGL-527H | Recombinant Human AGL Protein, MYC/DDK-tagged | +Inquiry |
AGL-2739H | Recombinant Human AGL protein(731-830 aa), C-His-tagged | +Inquiry |
Agl-1554M | Recombinant Mouse Agl Protein, Myc/DDK-tagged | +Inquiry |
AGL-290H | Recombinant Human AGL Protein, His (Fc)-Avi-tagged | +Inquiry |
Agl-93M | Recombinant Mouse Agl Protein, His-tagged | +Inquiry |
◆ Lysates | ||
AGL-8980HCL | Recombinant Human AGL 293 Cell Lysate | +Inquiry |
AGL-8979HCL | Recombinant Human AGL 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (20)
Ask a questionYes, AGL mutations can cause low blood sugar levels due to impaired glucose release.
AGL mutations might contribute to cardiomyopathy due to glycogen accumulation.
Yes, AGL mutations can lead to muscle weakness due to impaired glycogen breakdown.
Research explores whether AGL's function is conserved in different organisms.
AGL activity ensures proper glycogen breakdown, maintaining cellular glycogen levels.
Yes, ongoing research uncovers AGL's roles in metabolism and related diseases.
AGL's enzymatic activity alters glycogen structure by removing branches.
AGL's role in glycogen metabolism makes it a potential therapeutic target.
AGL's enzymatic role is in breaking down glycogen, not synthesizing it.
AGL dysfunction can affect various tissues due to glycogen storage disruptions.
AGL deficiency affects muscle cells due to impaired glycogen breakdown.
Research on AGL provides insights into glycogen metabolism and related diseases.
Yes, hormones regulate AGL activity to maintain glucose levels.
Yes, AGL's role in glycogen breakdown can impact heart function and health.
AGL's role in glycogen breakdown helps maintain glucose homeostasis.
Yes, AGL deficiency is usually inherited in an autosomal recessive manner.
AGL deficiency hinders glucose release from glycogen, affecting energy supply.
Yes, AGL mutations can impact exercise tolerance due to limited energy supply.
Yes, AGL mutations can impact multiple organs due to glycogen storage issues.
AGL mutations can impact brain health due to glycogen storage issues in certain tissues.
Customer Reviews (5)
Write a reviewNotable improvements in cell proliferation were attributed to the protein product’s efficacy.
We observed a significant enhancement in enzyme activity using the protein product.
The protein product’s compatibility with various assays broadened the scope of our investigations.
Reliable protein-protein interaction studies were enabled by the protein product’s pure composition.
Minimal background noise in our assays indicated the protein product’s quality.
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