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The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Rat CLEC14A ORF mammalian expression plasmid, C-GFPSpark tag||RG80211-ACG|
|Rat CLEC14A ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80211-ACR|
|Rat CLEC14A ORF mammalian expression plasmid, C-Flag tag||RG80211-CF|
|Rat CLEC14A ORF mammalian expression plasmid, C-His tag||RG80211-CH|
|Rat CLEC14A ORF mammalian expression plasmid, C-Myc tag||RG80211-CM|
|Rat CLEC14A ORF mammalian expression plasmid, C-HA tag||RG80211-CY|
|Rat CLEC14A ORF mammalian expression plasmid, N-Flag tag||RG80211-NF|
|Rat CLEC14A ORF mammalian expression plasmid, N-His tag||RG80211-NH|
|Rat CLEC14A ORF mammalian expression plasmid, N-Myc tag||RG80211-NM|
|Rat CLEC14A ORF mammalian expression plasmid, N-HA tag||RG80211-NY|
|Rat CLEC14A natural ORF mammalian expression plasmid||RG80211-UT|
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C-type lectin domain family 14 member A, also known as Epidermal growth factor receptor 5 and CLEC14A, is a member of the C-type lectin domain (CTLD) family that contains one c-type lectin domain and one EGF-like domain. Mouse CLEC14A is a 459 amino acid single-pass type I membrane protein. The superfamily of proteins containing C-type lectin-like domains (CTLDs) is a large group of extracellular Metazoan proteins with diverse functions. The CTLD structure has a characteristic double-loop ('loop-in-a-loop') stabilized by two highly conserved disulfide bridges located at the bases of the loops, as well as a set of conserved hydrophobic and polar interactions. Members of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily share a common fold and are involved in a variety of functions, such as generalized defense mechanisms against foreign agents, discrimination between healthy and pathogen-infected cells, and endocytosis and blood coagulation. Genome-level studies on human, elegans and melanogaster demonstrated almost complete divergence among invertebrate and mammalian families of CTLD-containing proteins (CTLDcps). The vertebrate CTLDcp families were essentially formed early in vertebrate evolution and are completely different from the invertebrate families. The composition of the CTLDcp superfamily in fish and mammals suggests that large scale duplication events played an important role in the evolution of vertebrates.