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The protein encoded by AP1M1 is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. Additionally we are shipping AP1M1 Antibodies (56) and AP1M1 Proteins (5) and many more products for this protein.
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L-selectin is transported constitutively by the AP-1 complex, leading to the formation of a trans-Golgi network reserve pool; phosphorylation of the L-selectin tail blocks AP-1-dependent retrograde transport of L-selectin
In mu1A-adaptin-deficient fibroblasts, MPR300-mediated endocytosis is markedly enhanced by a mechanism not associated with increased steady-state concentration of receptors at the plasma membrane, but with an increased internalization rate of MPR300.
Here, the authors demonstrate that dileucine motifs in the hepatitis C virus NS2 protein mediate AP-1A, AP-1B, and AP-4 binding and cell-free virus release. Moreover, they reveal that AP-4, an adaptor not previously implicated in viral infections, mediates cell-to-cell spread and hepatitis C virus trafficking.
found 31 ORF9p interaction partners, among which was AP1M1, the mu subunit of the adaptor protein complex 1 (AP-1). AP-1 is a heterotetramer involved in intracellular vesicle-mediated transport and regulates the shuttling of cargo proteins between endosomes and the trans-Golgi network via clathrin-coated vesicles.
Acidic clusters act as sorting signals for packaging cargo into clathrin-coated vesicles (CCVs), and also facilitate down-regulation of MHC-I by HIV-1 Nef. The basic patch on micro1 that interacts with the Nef acidic cluster also contributes to the binding of endogenous acidic cluster proteins.
CNNM4 is sorted to the basolateral membrane by the complementary function of AP-1A and AP-1B
Adaptor protein 1 promotes cross-presentation through the same tyrosine signal in major histocompatibility complex class I as that targeted by HIV-1.
IRS-1 associates with mu1A of the ubiquitously expressed AP-1 complex through three protein interaction motifs.
Mu1A binding to the N terminus of HIV-1 Nef determines its ability to downregulate major histocompatibility complex class I in T lymphocytes.
AP-1 mu1A is involved in the kAE1 trafficking of kidney alpha-intercalated cells
These data identify the micro subunit of AP-1 (micro1) as the key target of the MHC-I CD/Nef complex, and they indicate that both Y320 in the MHC-I CD and E62-65 in Nef interact directly with micro1.
The protein encoded by this gene is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. The other components of this complex are beta-prime-adaptin, gamma-adaptin, and the small chain AP1S1. This complex is located at the Golgi vesicle and links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing. Alternatively spliced transcript variants encoding distinct protein isoforms have been found for this gene.
AP-1 complex subunit mu-1
, AP-mu chain family member mu1A
, adaptor protein complex AP-1 mu-1 subunit
, adaptor-related protein complex 1 mu-1 subunit
, clathrin assembly protein complex 1 medium chain 1
, clathrin coat assembly protein AP47
, clathrin coat-associated protein AP47
, golgi adaptor HA1/AP1 adaptin mu-1 subunit
, mu-adaptin 1
, HA1 47 kDa subunit
, clathrin adaptor protein AP47
, clathrin assembly protein complex 1, medium chain
, clathrin assembly protein complex AP1, mu subunit
, golgi adaptor AP-1 47 kDa protein
, adaptor-related protein complex AP-1, mu subunit 1
, adaptor related protein complex 1 mu 1 subunit S homeolog
, adaptor-related protein complex 1, mu 1 subunit