Analytical Data
-
Gene name
HNMT
- Application
-
Alternative Names
HNMT;Histamine N-methyltransferase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P50135
-
Expression Region
1-292aa
-
AA Sequence
MASSMRSLFS DHGKYVESFR RFLNHSTEHQ CMQEFMDKKL PGIIGRIGDT KSEIKILSIG GGAGEIDLQI LSKVQAQYPG VCINNEVVEP SAEQIAKYKE LVAKTSNLEN VKFAWHKETS SEYQSRMLEK KELQKWDFIH MIQMLYYVKD IPATLKFFHS LLGTNAKMLI IVVSGSSGWD KLWKKYGSRF PQDDLCQYIT SDDLTQMLDN LGLKYECYDL LSTMDISDCF IDGNENGDLL WDFLTETCNF NATAPPDLRA ELGKDLQEPE FSAKKEGKVL FNNTLSFIVI EA
-
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
HNMT (Histamine N-Methyltransferase) is a crucial enzyme involved in the metabolism of histamine, a biogenic amine that plays significant roles in allergic responses, neurotransmission, and regulation of physiological functions. The deregulation of histamine levels has been linked to various pathological conditions, including allergies, asthma, and neurological disorders. Understanding HNMT's function and regulation is essential for developing potential therapeutic strategies to modulate histamine-related diseases. Recent advances in recombinant protein technology have enabled the expression and purification of HNMT in heterologous systems, facilitating detailed biochemical and structural studies. This research aims to elucidate the enzyme's kinetics, structural dynamics, and interaction with potential inhibitors. By producing HNMT as a recombinant protein, scientists can explore its role in histamine metabolism more effectively and screen for small molecules that may enhance or inhibit its activity. This research not only contributes to our understanding of histamine biology but also opens avenues for drug discovery and the development of novel treatments for conditions associated with histamine dysregulation.
