Recombinant Human TPM4 Protein (His Tag)

Name: Recombinant Human TPM4 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4615
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P67936
Synonym	HEL-S-108, TPM4
Background	TPM4, also known as tropomyosin 4, is a member of the tropomyosin family. Members of this family are actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. TPM4 is expressed in cardiac tissue and platelets. It is highly expressed in the platelets of hypertensive patients. TPM4 plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells it is implicated in stabilizing cytoskeleton actin filaments.
Description	A DNA sequence encoding the human TPM4 (P67936) (Ala2-Ile248) was expressed with an N-terminal His tag.
Source	HEK293
Predicted N Terminal	His
AA Sequence	Ala2-Ile248
Molecular Weight	The recombinant human TPM4 comprises 267 a.a. and has a predicted molecular mass of 30.8 kDa. The apparent molecular mass of the protein is approximately 35-40 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium.
Subcellular Location	Cytoplasm, cytoskeleton.
Protein Families	Tropomyosin family
Database References	HGNC: 12013 OMIM: 600317 KEGG: hsa:7171 UniGene: Hs.631618
Tissue Specificity	Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets o

Gene Functions References

TPM4 is associated with clinical progression in colon cancer patients and acts as a tumor suppressor in colon cancer cells. PMID: 29455030
Tpm4.1 is essential to maintain cell-cell adhesions and to inhibit abnormal increases in cell migration and invasion, which are important to prevent invasion and metastasis of breast cancer cells. PMID: 28431393
findings demonstrate a nonredundant role for TPM4 in platelet biogenesis in humans and mice and reveal that truncating variants in TPM4 cause a previously undescribed dominant Mendelian platelet disorder. PMID: 28134622
Results show that Tpm4.2 facilitates the transition of NM-2A to the strongly actin-binding myosin-ADP state. PMID: 26847712
Data indicate the upregulation of tropomyosin-4 in infiltrating ductal breast carcinomas (IDCAs) tissues, which may suggest its involvement in breast cancer development. PMID: 23812729
TPM4, PDIA and SRC8 were also localized to the trophoblast cells, further highlighting the importance of these cytoskeletal remodelling proteins in early pregnancy PMID: 21373848
Low TPM4 expression in the cytoplasm is associated with uterine cervix carcinogenesis. PMID: 21119665
Tm4-defined cytoskeleton is a marker of growth and repair/regeneration in response to injury, disease state and stress in skeletal muscle. PMID: 17968984

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.