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The protein encoded by MANF is localized in the endoplasmic reticulum (ER) and golgi, and is also secreted. Additionally we are shipping MANF Antibodies (93) and MANF Kits (22) and many more products for this protein.
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Human MANF Protein expressed in Human Cells - ABIN2004225
Shridhar, Rivard, Shridhar, Mullins, Bostick, Sakr, Grignon, Miller, Smith: A gene from human chromosomal band 3p21.1 encodes a highly conserved arginine-rich protein and is mutated in renal cell carcinomas. in Oncogene 1996
Show all 3 references for ABIN2004225
Mouse (Murine) MANF Protein expressed in Human Cells - ABIN2008442
Gevaert, Goethals, Martens, Van Damme, Staes, Thomas, Vandekerckhove: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. in Nature biotechnology 2003
Show all 3 references for ABIN2008442
Human MANF Protein expressed in Escherichia coli (E. coli) - ABIN1098235
Petrova, Raibekas, Pevsner, Vigo, Anafi, Moore, Peaire, Shridhar, Smith, Kelly, Durocher, Commissiong: MANF: a new mesencephalic, astrocyte-derived neurotrophic factor with selectivity for dopaminergic neurons. in Journal of molecular neuroscience : MN 2003
Show all 2 references for ABIN1098235
These data suggest a role for Manf in the regulation of Drosophila unfolded protein response.
DmMANF expression in the adult brain is much wider than in the embryonic and larval stages. It is expressed in both glia and neurons including dopaminergic neurons.
study offers further insights into the functional conservation between invertebrate and mammalian MANF/CDNF (show CDNF Proteins) proteins and reveals the importance of the C-terminal domain for MANF activity in vivo
role of MANF in multicellular organism development
DmMANF is an invertebrate neurotrophic factor (show NTF3 Proteins) supporting dopaminergic neurons.
These results suggest that MANF is involved in the regulation of the development of dopaminergic system in zebrafish.
the role of two short sequence motifs within the carboxy-(C) terminal domain of MANF in its neuroprotective activity, was studied.
the selective expression of MANF in splenocytes may be involved in plasma cell differentiation and immune regulation.
MANF is a protein that interacts with RTN1-C (show RTN1 Proteins)
We demonstrate that Armet and Creld2 (show CRELD2 Proteins) are genotype-specific ER stress response proteins with substrate specificities, and that aggregation of mutant matrilin-3 (show MATN3 Proteins) is a key disease trigger in MED that could be exploited as a potential therapeutic target
MANF binding to the plasma membrane also required the RTDL sequence and was inhibited with a peptide known to interact with KDELRs, suggesting MANF binds KDELRs at the surface.
MANF and C-MANF protect neurons intracellularly as efficiently as Ku70.
Pretreatment with adeno (show ADORA2A Proteins)-associated-virus vector containing human MANF reduces the volume of cerebral infarction and facilitates behavioral recovery in experimental stroke rats.
Armet is a novel secreted mediator of the adaptive pathway of unfolded protein response.
The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggest that it has important functions both under normal and pathological conditions in many tissue types.
structures of MANF and CDNF (show CDNF Proteins) were solved; structure explains why MANF and CDNF (show CDNF Proteins) are bifunctional; neurotrophic activity may reside in the N-terminal domain and ER stress response in the C-terminal domain
MANF has immune modulatory properties that are required for retinal repair in Drosophila
secretion of mouse MANF and mouse CDNF (show CDNF Proteins) is fundamentally regulated in the same manner, the variation of four C-terminal amino acids in the MANF and CDNF (show CDNF Proteins) among species might influence their intracellular functions.
MANF-deficient mice develop severe diabetes, progressive postnatal reduction of beta cell mass and chronic unfolded protein response activation.
Secretion of MANF is regulated via COPII-mediated transport and that its C-terminus could be responsible for its retention in the endoplasmic reticulum through GRP78 (show HSPA5 Proteins).
The change in Armet expression lasted while the change of Mrpl51 (show MRPL51 Proteins) disappeared after birth.
the solution structure of ARMET
ARMET is the second fully characterized ERSE-II-dependent gene and likely contributes to quality control of proteins in the endoplasmic reticulum
The protein encoded by this gene is localized in the endoplasmic reticulum (ER) and golgi, and is also secreted. Reducing expression of this gene increases susceptibility to ER stress-induced death and promotes cell proliferation. The protein was initially thought to be longer at the N-terminus and to contain an arginine-rich region but transcribed evidence indicates a smaller open reading frame that does not encode the arginine tract. The presence of polymorphisms in the arginine-rich region, including a specific mutation that changes the previously numbered codon 50 from ATG to AGG, have been reported in a variety of solid tumors\; however, these polymorphisms were later shown to exist in normal tissues and are thus not tumor-related.
mesencephalic astrocyte-derived neurotrophic factor
, arginine-rich, mutated in early stage tumors
, arginine-rich protein
, RNA binding motif protein 15B
, chromosome 3p21.1 gene sequence