|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Human PRSS27 ORF mammalian expression plasmid, C-GFPSpark tag||HG12116-ACG|
|Human PRSS27 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG12116-ACR|
|Human PRSS27 ORF mammalian expression plasmid, C-Flag tag||HG12116-CF|
|Human PRSS27 ORF mammalian expression plasmid, C-His tag||HG12116-CH|
|Human PRSS27 ORF mammalian expression plasmid, C-Myc tag||HG12116-CM|
|Human PRSS27 ORF mammalian expression plasmid, C-HA tag||HG12116-CY|
|Human PRSS27 Gene cDNA clone plasmid||HG12116-G|
|Human PRSS27 ORF mammalian expression plasmid, N-Flag tag||HG12116-NF|
|Human PRSS27 ORF mammalian expression plasmid, N-His tag||HG12116-NH|
|Human PRSS27 ORF mammalian expression plasmid, N-Myc tag||HG12116-NM|
|Human PRSS27 ORF mammalian expression plasmid, N-HA tag||HG12116-NY|
|Human PRSS27 natural ORF mammalian expression plasmid||HG12116-UT|
|Learn more about expression Vectors|
The name "Pancreasin" because it is transcribed strongly in the pancreas. This secreted, tryptic serine protease, also known as Marapsin or PRSS27 (Protease, serine, 27), which is a member of the peptidase S1 family. Pancreasin is inhibited by benzamidine and leupeptin but resists several classic inhibitors of trypsin. Marapsin was constitutively expressed in nonkeratinizing stratified squamous epithelia of human esophagus, tonsil, cervix, larynx, and cornea. In fact, marapsin was the second most strongly up-regulated protease in psoriatic lesions, where expression was localized to the upper region of the hyperplastic epidermis. Similarly, in the hyperproliferative epithelium of regenerating murine skin wounds, marapsin localized to the suprabasal layers, where keratinocytes undergo squamous differentiation. Marapsin's restricted expression, localization, and cytokine-inducible expression suggest a role in the terminal differentiation of keratinocytes in hyperproliferating squamous epithelia.