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What are the 4 fibroblast growth factor receptors?

The human fibroblast growth factor receptor (FGFR) family consists of four members: FGFR1 to FGFR4. Despite being encoded by separate genes, the four members share high homology, with their sequence identity varying from 56% to 71% [1].

How would we classify the FGF fibroblast growth factor )?

Fgfs have been identified in metazoans but not in unicellular organisms. In vertebrates, FGFs can be classified as having intracrine, paracrine and endocrine functions. Paracrine and endocrine FGFs act via cell-surface FGF receptors (FGFRs); while, intracrine FGFs act independent of FGFRs.

What are the different types of FGFR?

So far, five distinct membrane FGFR have been identified in vertebrates and all of them belong to the tyrosine kinase superfamily (FGFR1 to FGFR4). FGFR1 (see also Fibroblast growth factor receptor 1) (= CD331) FGFR2 (see also Fibroblast growth factor receptor 2) (= CD332)

How many FGFs are there?

In vertebrates, the 22 members of the FGF family range in molecular mass from 17 to 34 kDa and share 13-71% amino acid identity. Between vertebrate species, FGFs are highly conserved in both gene structure and amino-acid sequence.

What are the different types of FGF receptors?

Fibroblast growth factor receptor (FGFR) belongs to the super-family of receptor tyrosine kinases and is encoded by four genes (FGFR1, FGFR2, FGFR3, and FGFR4).

What is the solubility of bFGF?

Solubility. It is recommended to reconstitute the lyophilized Fibroblast Growth Factor Basic in sterile 18M-cm H2O not less than 100g/ml, which can then be further diluted to other aqueous solutions.

What are the different types of fibroblast growth factors?

The mammalian fibroblast growth factor receptor family has 4 members, FGFR1, FGFR2, FGFR3, and FGFR4.

What are the domains of FGF receptors?

FGF receptors are single-pass membrane proteins, with N-terminal extracellular (EC) domains consisting of three immunoglobulin-like subdomains (D1, D2 and D3), a transmembrane (TM) domain consisting of a single -helix, and an intracellular (IC) region encompassing a tyrosine kinase domain16,17,18.

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