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Regenerative & CytoprotectiveOpen access · public

Follistatin-344

Follistatin-344 (FST-344) is the longer alternatively-spliced isoform of human follistatin, a secreted regulatory glycoprotein encoded by the FST gene (canonical UniProt P19883).

UniProt P19883Type ProteinResearch Use Only · reference
Representative ribbon structure of Follistatin-344 (PDB 2P6A)
Representative follistatin structure (PDB 2P6A, follistatin in complex with activin). Illustrative of the follistatin fold; not a structure of the 344 isoform specifically.

Identity & structure

Amino-acid sequence · 344 aa
MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW
  • Signal peptide (residues 1–29; removed in the mature FS-315 chain)

344-residue primary translation product, including the 29-residue signal peptide (residues 1–29). After signal-peptide cleavage the mature secreted protein is 315 residues (FS-315, residues 30–344) — the “344” is a precursor count, not a mature-chain length.

Follistatin-344 — identity and specification
Identity
TypeProtein
Also known asFST-344, FS-344, Follistatin 344, Follistatin isoform FST344, Activin-binding protein, Follistatin, FST
CASNot asserted — not cleanly resolved to this isoform (pending verification)
PubChem CIDNot assigned — a protein of this size receives no small-molecule PubChem CID
UniProtP19883 — canonical 344-aa isoform
Research classRegenerative & Cytoprotective
Structure
Length344 aa (precursor); mature chain 315 aa
Molecular formulaNot applicable — glycoprotein; mass heterogeneous
InChIKeyNot assigned — proteins are outside InChI’s practical domain
PDB2P6A, 2B0U
Analytical
Monoisotopic massNot applicable — glycoprotein; mass heterogeneous

Mass basis (glycoprotein — no single exact mass)

  • 344-aa precursor, unglycosylated (incl. signal peptide)38,006.79 Da (UniProt calc.)
  • Mature FS-315 polypeptide (res 30–344), unglycosylated~34.7 kDa (calc.)
  • Native/recombinant glycoprotein (SDS-PAGE apparent)~40–50 kDa

Follistatin is heavily disulfide-bonded (every cysteine is paired) and glycosylated: recombinant mature follistatin migrates at roughly 40–50 kDa on SDS-PAGE, above its ~34.7 kDa polypeptide mass, because of attached N-linked glycans (N-X-S/T sequons in the precursor). Because the glycans are heterogeneous, no single exact molecular formula, monoisotopic mass, or InChIKey applies; the identity is captured by the sequence and the UniProt and PDB cross-references.

Reference context

Follistatin-344 (FST-344) is the longer alternatively-spliced isoform of human follistatin, a secreted regulatory glycoprotein encoded by the FST gene (canonical UniProt P19883). The “344” is the length in amino acids of the primary translation product, counting the 29-residue signal peptide; once that signal peptide is removed, the mature secreted protein is 315 residues (FS-315, residues 30–344). A shorter splice isoform gives the 288-residue mature form (FS-288), and a C-terminally truncated proteolytic product is known as FS-303 — so the “344” label specifically denotes the longer precursor, not a 344-residue mature chain. Follistatin is heavily disulfide-bonded (every cysteine is paired) and, importantly, it is glycosylated: recombinant mature follistatin migrates at roughly 40–50 kDa on SDS-PAGE, above its ~34.7 kDa polypeptide mass, because of attached N-linked glycans. That glycosylation makes the protein’s mass heterogeneous, so no single exact molecular formula or monoisotopic mass describes it — its identity is captured instead by its sequence, its UniProt and PDB cross-references, and a stated mass range. At the molecular level, follistatin is characterized as a high-affinity binding partner for activin and related TGF-β-superfamily ligands; the deposited crystal structure of the follistatin–activin complex shows two follistatin molecules encircling the activin dimer. Lineará lists Follistatin-344 as a characterization-only reference entity. For Research Use Only — Not for Human or Veterinary Use.

Listed solely as a characterized analytical reference — no representation is made as to any biological effect. For Research Use Only — not for human or veterinary use.

How Follistatin-344 is characterized

For a folded protein, identity rests on the amino-acid sequence and its cross-references rather than a small-molecule structure. The sequence above is the anchor identifier; the UniProt accession and the representative Protein Data Bank entries locate the fold. Because the native protein is glycosylated, its mass is heterogeneous: it is stated as a labeled basis (calculated polypeptide mass and apparent mass by SDS-PAGE), not a single number, and no single molecular formula or monoisotopic mass applies.

IdentityAmino-acid sequence · UniProt P19883
StructurePDB ribbon · 2P6A, 2B0U
MassBasis/range · glycoprotein

Frequently asked questions

What is Follistatin-344?
Follistatin-344 (FST-344) is the longer splice isoform of human follistatin, a secreted regulatory glycoprotein. The “344” counts the amino acids of the precursor, including its 29-residue signal peptide; the mature protein is 315 residues (FS-315), not 344.
What is the difference between FS-344, FS-315, FS-288 and FS-303?
FS-344 and FS-317 are the two splice-isoform precursors (with signal peptide). Removing the signal peptide gives the mature forms FS-315 (from FS-344) and FS-288 (from FS-317). FS-303 is a shorter, C-terminally truncated proteolytic product.
What is the molecular weight of Follistatin-344?
The unglycosylated 344-residue precursor calculates to about 38,007 Da, and the mature FS-315 polypeptide to about 34.7 kDa. Because the native protein is glycosylated, it runs heavier and heterogeneously — roughly 40–50 kDa on SDS-PAGE.
Does Follistatin-344 have a single molecular formula?
No. Follistatin is a glycoprotein with variable attached sugar chains, so its mass is heterogeneous and no single exact molecular formula, monoisotopic mass, or InChIKey applies. It is identified by its sequence and its UniProt (P19883) and PDB cross-references instead.
What does follistatin bind at the molecular level?
Follistatin is characterized as a high-affinity binding partner for activin and other TGF-β-superfamily ligands. Structural studies of the follistatin–activin complex show two follistatin molecules wrapping around an activin dimer.
Is Follistatin-344 a peptide?
Not exactly. Follistatin-344 is a protein — a larger polypeptide of 344 residues. It is built from amino acids like a peptide, but is longer and adopts a defined folded structure.
How is Follistatin-344 stored and reconstituted?
As a research material, Follistatin-344 is typically handled as a lyophilized (freeze-dried) powder. It is kept desiccated and cold — commonly 2–8 °C for short periods and −20 °C for longer storage — and reconstituted in sterile or bacteriostatic water. This is storage and handling information only, not a use protocol.
Does Lineará sell Follistatin-344?
No. Follistatin-344 is listed here only as a characterization reference entity. It is not part of the Lineará formulary, has no price or certificate of analysis, and is not offered for sale.
Is Follistatin-344 approved for human use?
No. Follistatin-344 is presented strictly as characterization reference data. It is not a drug, is not approved for any human or veterinary use, and must not be administered to humans or animals.

Data, tools & related references

References

  1. UniProt — protein sequence & annotation (P19883). UniProt →
  2. RCSB Protein Data Bank — representative structures (2P6A, 2B0U).

Research professionals only

Reference data

This monograph is characterization reference data. Lineará does not sell, stock, or certify Follistatin-344.

áFor Research Use Only · Not for human or veterinary use · Not for diagnostic or therapeutic use