Analytical Data
-
Gene name
NMB
- Application
-
Alternative Names
GPNMB;HGFIN;NMB;Transmembrane glycoProtein NMB
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P08949
-
Expression Region
1-121aa
-
AA Sequence
MARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK
-
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
NMB, or Neuromedin B, is a neuropeptide that belongs to the bombesin-like peptide family and plays a crucial role in various physiological processes, including the regulation of stress responses, appetite control, and respiratory functions. It is primarily produced in the central nervous system and gastrointestinal tract, where it interacts with specific receptors, such as the neuromedin B receptor (NMBR). Research on NMB and its recombinant protein has gained significant attention due to its potential implications in understanding metabolic disorders, obesity, and cancer. The study of NMB also holds promise for therapeutic applications, particularly in targeting the neuroendocrine pathways associated with these conditions. Recombinant DNA technology has enabled the production of NMB in a laboratory setting, allowing for detailed studies on its structure, function, and interaction with other molecules. Moreover, the development of recombinant NMB provides a valuable tool for investigating its biological activity and potential as a drug candidate. As research continues to unveil the intricacies of NMB signaling pathways, it may pave the way for novel treatment strategies and enhance our understanding of the neuropeptide's role in health and disease.











