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Sequence Information

Transthyretin (TTR) Recombinant Protein | TTR recombinant protein

Recombinant Transthyretin (TTR)

Gene Names
TTR; CTS; CTS1; PALB; TBPA; HEL111; HsT2651
Applications
SDS-Page, Western Blot, ELISA, Immunoprecipitation
Purity
> 95%
Synonyms
Transthyretin (TTR); Recombinant Transthyretin (TTR); TTR recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
> 95%
Form/Format
Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
Sequence
The target protein is fused with a N-terminal his-tag, its sequence is listed below.
MGHHHHHHSGSEF-GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS GPRRYTIAAL LSPYSYSTTA VVTNPKE
Sequence Length
147
Applicable Applications for TTR recombinant protein
SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
Organism
Homo sapiens (Human)
Expression System
Prokaryotic expression
Residues
Gly21~Glu147 (Accession # P02766) with a N-terminal his-tag
Endotoxin Level
<1.0EU per 1ug (determined by the LAL method)
Reconstitution
Reconstitute in sterile PBS, pH7.2-pH7.4.
Preparation and Storage
Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

Sequence Information

Sequence Information

SDS-Page

SDS-Page

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
15.3kDa
NCBI Official Full Name
transthyretin
NCBI Official Synonym Full Names
transthyretin
NCBI Official Symbol
TTR
NCBI Official Synonym Symbols
CTS; CTS1; PALB; TBPA; HEL111; HsT2651
NCBI Protein Information
transthyretin; ATTR; carpal tunnel syndrome 1; thyroxine-binding prealbumin; epididymis luminal protein 111; prealbumin, amyloidosis type I
UniProt Protein Name
Transthyretin
Protein Family
UniProt Gene Name
TTR
UniProt Synonym Gene Names
PALB
UniProt Entry Name
TTHY_HUMAN

NCBI Description

This gene encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Transthyretin is a carrier protein; it transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. The protein consists of a tetramer of identical subunits. More than 80 different mutations in this gene have been reported; most mutations are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart, and a small portion of the gene mutations is non-amyloidogenic. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc. [provided by RefSeq, Jan 2009]

Uniprot Description

TTR: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR). A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. Defects in TTR are a cause of hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE). It is a condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. Defects in TTR are a cause of carpal tunnel syndrome type 1 (CTS1). It is a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Belongs to the transthyretin family.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 18q12.1

Cellular Component: extracellular space; protein complex; cytoplasm; extracellular region

Molecular Function: identical protein binding; protein binding; protein heterodimerization activity; hormone activity

Biological Process: phototransduction, visible light; extracellular matrix organization and biogenesis; transport; retinol metabolic process; retinoid metabolic process

Disease: Hyperthyroxinemia, Dystransthyretinemic; Carpal Tunnel Syndrome; Amyloidosis, Hereditary, Transthyretin-related

Research Articles on TTR

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Product Notes

The TTR ttr (Catalog #AAA2009028) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's Transthyretin (TTR) can be used in a range of immunoassay formats including, but not limited to, SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP). Researchers should empirically determine the suitability of the TTR ttr for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: The target protein is fused with a N-terminal his-tag, its sequence is listed below. MGHHHHHHSG SEF-GPTGTG ESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS GPRRYTIAAL LSPYSYSTTA VVTNPKE. It is sometimes possible for the material contained within the vial of "Transthyretin (TTR), Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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