Analytical Data
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Gene name
AP1m2
- Application
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Alternative Names
HSMU1B; MU-1B; MU1B; Clathrin assembly protein complex 1 mu-2 medium chain 2; Golgi adaptor HA1/AP1 adaptin mu-2 subunit; AP-mu chain family member mu1B
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y6Q5
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Expression Region
Met1~Met207
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Molecular Weight
27kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
AP1M2, or Adaptor Protein Complex 1 Mu2 Subunit, is a key component of the clathrin-coated vesicles involved in cellular trafficking. Research on AP1M2 has gained attention due to its crucial role in endosomal and lysosomal transport processes, which are vital for maintaining cellular homeostasis and regulating the turnover of membrane proteins. Mutations or dysregulation of AP1M2 have been implicated in various diseases, including neurodegenerative disorders and certain types of cancer, as they can disrupt normal cellular communication and waste management processes. Additionally, the protein's involvement in the sorting and delivery of cargo, such as receptors and enzymes, highlights its potential as a biomarker for disease progression. Understanding the structure and function of AP1M2, especially through studies involving recombinant protein techniques, can provide insights into its mechanistic role in these cellular processes. Furthermore, the refinement of methods to produce AP1M2 as a recombinant protein facilitates detailed biochemical analyses and offers opportunities for therapeutic interventions targeting AP1M2-related pathways. As such, ongoing research aims to unravel the complexities of AP1M2 interactions, its regulatory mechanisms, and its potential as a target for novel treatment strategies in disease contexts where cellular trafficking is disrupted.
