Name: Thymosin Alpha 1 10mg (Research Peptide)
Brand: Verum Peptides
Price: 99 USD
Availability: InStock

Identification

Chemical name	N-acetylated 28-residue peptide corresponding to the N-terminal region of prothymosin alpha
Common designations	Thymosin alpha 1; Tα1; thymalfasin
Sequence	Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn
Length	28 amino acids, N-terminally acetylated
Molecular formula	C129H215N33O55
Molecular weight	3108.3 g/mol
Expected ions	[M+3H]3+ near 1037; [M+4H]4+ near 778
CAS number	62304-98-7
Charge profile	Strongly acidic. Nine aspartate and glutamate residues against five lysines, with the N-terminal amine blocked by acetylation.
Oxidation-sensitive residues	None. The sequence contains no methionine, cysteine, tryptophan or tyrosine.
Physical form	White lyophilized powder
Quantity supplied	10 mg nominal per unit
Country of manufacture	United States

Certificate of analysis - current lot

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Certificate of analysis - lot THYMA10-042026-1

Lot record

THYMA10-042026-1

Testing laboratory	Freedom Diagnostics, United States. Independent third party, not owned by or affiliated with Verum.
Sample received	14 April 2026
Results reported	15 April 2026
Accession reference	2604140268
Analytical methods	HPLC-UV coupled to mass spectrometry (LC-MS). Bacterial endotoxin by limulus amebocyte lysate assay in accordance with USP .

Results, this lot

Identity, LC-MS	Confirmed as thymosin alpha-1, named in full on the certificate
Purity, HPLC-UV	99.65 %
Net peptide content	11.87 mg per unit
Appearance	White lyophilized powder
Bacterial endotoxin	Pass, duplicate replicates. Assay sensitivity ≤0.05 EU/mL
Mass confirmation	Ions at m/z 778.0 [M+4H]4+ and 1037.0 [M+3H]3+. Reconstructed independently both give 3108, against an expected 3108.3.

Purity, content and endotoxin figures above are specific to lot THYMA10-042026-1 and are not specifications carried across other lots. Two independent charge states landing on the same molecular weight is a stronger identity argument than a single ion, because a truncated or deacetylated species shifts both rather than hiding inside one peak.

The acetyl group is part of the molecule, not a detail

This peptide is acetylated at its N-terminus, and the modification is not cosmetic. It blocks the free amine that aminopeptidases would otherwise attack, and it removes a positive charge from a molecule that is already strongly acidic. A preparation of the same 28 residues without that acetyl group is a different compound with a different charge state, different stability and a molecular weight 42 daltons lower.

That is a difference the mass detects and a purity percentage does not. Forty-two daltons on a 3108 molecule is a shift of about 1.4 percent, which a competent instrument resolves cleanly and which a single retention time will not. The certificate above reports two charge states, both landing on 3108, so the acetylation is accounted for. It is worth checking on any supplier's certificate rather than assuming, because deacetylated material will still look like a clean peak.

Testing scope

Panels differ between products and between lots. What follows is the scope of testing performed on this lot. Nothing is claimed unless it appears on the certificate for the lot supplied.

Performed

✓	Identity by LC-MS
✓	Purity by HPLC-UV
✓	Net peptide content
✓	Appearance by visual inspection
✓	Mass confirmation, two charge states
✓	Bacterial endotoxin, USP , duplicate

Not performed

-	N-terminal acetylation as a separate parameter
-	Deamidation profiling
-	Deletion sequence profiling
-	Sterility and microbial enumeration
-	Counterion identity and content
-	Elemental impurities, residual solvents

The first two entries in the right-hand column are the ones specific to this sequence. Acetylation is not reported as a separate parameter, though the observed mass accounts for it. Deamidation matters because a chain this rich in aspartate and glutamate, terminating in asparagine, has several sites at which it can occur, and each adds one dalton without changing the sequence. Where a parameter is material to intended laboratory work, purchasers should verify it independently or source material released against that specification.

Storage and laboratory handling

Lyophilized powder, transit	Stable at ambient temperature during shipping and short-term handling. Cold-chain transport is not required.
Lyophilized powder, storage	−20 °C, protected from light, container tightly closed
Solubility	Readily soluble in sterile laboratory-grade water or a defined aqueous buffer appropriate to the assay
Solution, storage	2 °C to 8 °C, protected from light. Materially less stable than the dry powder.
pH	Strongly acidic character in solution. Hold buffer conditions constant across an experiment rather than varying them between preparations, since solubility and behaviour shift with pH on a molecule carrying this many acidic residues.
Sequence-specific note	No oxidation-sensitive residues and a blocked N-terminus, so this sequence carries neither the oxidation liabilities nor the aminopeptidase vulnerability that govern many peptides. Both are genuine advantages and both are frequently overread: neither is stability in aqueous storage, and this peptide hydrolyses in solution like any other.
Freeze-thaw	Avoid repeated cycles. Aliquot at first preparation where the protocol allows.
Personal protection	Handle under standard laboratory conditions with gloves, eye protection and a laboratory coat.

Preparation conditions are the responsibility of the receiving laboratory. Verum provides no protocol, no preparation instruction, and no guidance on use.