Analytical Data
-
Gene name
HGD
- Application
-
Alternative Names
HGD；HGO；Homogentisate 1.2-dioxygenase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q93099
-
Expression Region
1-445aa
-
AA Sequence
MAELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFT CPRSTNKRSWLYRILPSVSHKPFESIDEGQVTHNWDEVDPDPNQLRWKPF EIPKASQKKVDFVSGLHTLCGAGDIKSNNGLAIHIFLCNTSMENRCFYNS DGDFLIVPQKGNLLIYTEFGKMLVQPNEICVIQRGMRFSIDVFEETRGYI LEVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQ GKLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTV LTAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGHY EAKQGGFLPGGGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMF ESSLSLAVTKWGLKASRCLDENYHKCWEPLKSHFTPNSRNPAEPN
-
Molecular Weight
54 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HGD, or Histidase, is an enzyme that plays a critical role in the catabolism of histidine, an essential amino acid. The study of recombinant HGD proteins has gained significant attention due to their potential applications in understanding metabolic disorders associated with histidine degradation, such as histidinemia, a rare genetic condition that can lead to neurological problems if left untreated. Advances in genetic engineering and recombinant DNA technology have made it feasible to produce HGD proteins in various host systems, allowing researchers to investigate the enzyme's structure, function, and regulation in detail. Furthermore, recombinant HGD can serve as a model for studying enzyme kinetics and the effects of mutations that may lead to deficiencies in histidine metabolism. Given the importance of histidine in various physiological processes, including neurotransmission and immune response, understanding the properties of recombinant HGD proteins can provide insights into metabolic pathways and their implications in health and disease. This research is particularly relevant as it may contribute to the development of novel therapeutic strategies for metabolic disorders and enhance our understanding of the fundamental mechanisms underlying amino acid catabolism.
