SECTM1 Human Recombinant Protein

Specifications

Product Data
Species	Human
Expression Host	CHO
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) Gln29-Gly145
Tag	C-His
Predicted MW	The protein has a predicted molecular weight of 14kDa and migrates at approximately 20kDa on SDS-PAGE with DTT-reduced condition before APC conjugation.
Concentration	25µg size is bottled at 0.1mg/mL concentration. 100 µg size is bottled at lot specific concentration.
Purity	>90%
Conjugation	APC
Buffer	1xPBS buffer, pH7.4, 0.09% NaN3 with a carrier protein
Preparation	Affinity Ni-NTA
Applications	FACS
Storage	An unopened vial can be stored at 4°C for 2 weeks or at -20°C and below for six months. This stock solution should be aliquoted and stored at ≤ -70°C to minimize the freeze/thaw cycles.
Stability	6 Months
Bioactivity	Positive The definition of the active protein (purified and biotinylated) is defined as the protein that can bind to its biological receptor/ligand. For conjugated protein, it is defined with its function to bind to the ScFv of the active CAR-transfected cells in flow cytometry test.
Reference Data
RefSeq	Q8WVN6
Locus ID	6398
UniProt ID	Q8WVN6
Summary	Human SECTM1 (secreted and transmembrance 1) is a type I transmembrane glycoprotein consisted of a 28 aa signal sequence, a 117 aa extracellular domain (ECD) with one potential N‑linked glycosylation site, a 21 aa transmembrane sequence, and an 82 aa cytoplasmic sequence. It is localized in the Golgi apparatus and exists as a transmembrane and a soluble form. SECTM1 protein expression is detected in some myeloid cells, such as stimulated monocytes, immature monocyte‑derived dendritic cells, and granulocytes. In the thymus, it is also expressed by epithelia and fibroblasts. Its expression is stimulated by IFN-gamma. Although its function is not well understood, the soluble N-terminus form of human SECTM1 demonstrates that it is a costimulatory ligand for human CD4 and CD8 T cell proliferation and cytokine production in CD7-dependent manner.
Protein Families	FACS

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