long-isoform

Insulin Receptor Protein, Human, Recombinant (long isoform, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 107 kDa and the accession number is P06213-1.

Insulin Receptor Protein, Human, Recombinant (long isoform, His), Biotinylated is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 107 kDa and the accession number is P06213-1.

Fatty Acid-Binding Protein 6 (FABP6) is cytoplasmic protein that binds long-chain fatty acids and other hydrophobic ligands which belongs to the calycin superfamily. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. FABP6 forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. It seems to be able to bind to bile salts and bilirubins.

Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.

SIRPB1A (Signal-regulatory protein beta 1A), also known as SIRP beta 1, belongs to signal-regulatory-protein (SIRP) family, and immunoglobulin superfamily. Signal-regulatory proteins (SIRPs) are cell-surface glycoproteins expressed on myeloid and neural cells that have been shown to recruit SH2 domain-containing protein phosphatase 1 (SHP-1) and SHP-2 and to regulate receptor tyrosine kinase-coupled signaling. SIRP are classified as SIRP alpha molecules, containing 11- to 113-amino acid long, or SIRP beta molecules, with a 5-amino acid long intracytoplasmic domain. SIRP beta 1 is a new DAP12-associated receptor involved in the activation of myeloid cells, which contains a short cytoplasmic domain that lacks sequence motifs capable of recruiting SHP-1 and SHP-2. SIRP beta 1 acts as an activating isoform of SIRP alpha molecules, confirming the co-existence of inhibitory ITIM-bearing molecules, recruiting SHP-1 and SHP-2 protein tyrosine phosphatases, and activating counterparts, whose engagement couples to protein tyrosine kinases via ITAM-bearing molecules.s