Recombinant Rat Serotransferrin (TF) Protein (His-KSI)

Name: Recombinant Rat Serotransferrin (TF) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-05213P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Serotransferrin (TF) Protein (His-KSI) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P12346
Target Symbol	TF
Synonyms	Tf; Serotransferrin; Transferrin; Beta-1 metal-binding globulin; Liver regeneration-related protein LRRG03; Siderophilin
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	VPDKTVKWCAVSEHENTKCISFRDHMKTVLPADGPRLACVKKTSYQDCIKAISGGEADAITLDGGWVYDAGLTPNNLKPVAAEFYGSLEHPQTHYLAVAVVKKGTDFQLNQLQGKKSCHTGLGRSAGWIIPIGLLFCNLPEPRKPLEKAVASFFSGSCVPCADPVAFPQLCQLCPGCGCSPTQPFFGYVGAFKCLRDGGGDVAFVKHTTIFEVLPQKADRDQYELLCLDNTRKPVDQYEDCYLARIPSHAVVARNGDGKEDLIWEILKVAQEHFGKGKSKDFQLFGSPLGKDLLFKDSAFGLLRVPPRMDYRLYLGHSYVTAIRNQREGVCPEGSIDSAPVKWCALSHQERAKCDEWSVSSNGQIECESAESTEDCIDKIVNGEADAMSLDGGHAYIAGQCGLVPVMAENYDISSCTNPQSDVFPKGYYAVAVVKASDSSINWNNLKGKKSCHTGVDRTAGWNIPMGLLFSRINHCKFDEFFSQGCAPGYKKNSTLCDLCIGPAKCAPNNREGYNGYTGAFQCLVEKGDVAFVKHQTVLENTNGKNTAAWAKDLKQEDFQLLCPDGTKKPVTEFATCHLAQAPNHVVVSRKEKAARVSTVLTAQKDLFWKGDKDCTGNFCLFRSSTKDLLFRDDTKCLTKLPEGTTYEEYLGAEYLQAVGNIRKCSTSRLLEACTFHKS
Expression Range	20-698aa
Protein Length	Full Length of Mature Protein
Mol. Weight	89.9 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Subcellular Location	Secreted.
Protein Families	Transferrin family
Database References	KEGG: rno:24825 STRING: 10116.ENSRNOP00000012725 UniGene: Rn.91296
Tissue Specificity	Expressed by the liver and secreted in plasma.

Gene Functions References

our data establish that blood TSAT exerts a critical role in experimental stroke-induced brain damage. In addition, our findings suggest that the protective effect of iron-free transferrin (apotransferrin, ATf) at the neuronal level resides in preventing NMDA-induced HTf uptake and ROS production, which in turn reduces neuronal damage PMID: 29248829
In brain interstitial fluid, transferrin-bound iron and non-transferrin-bound iron (NTBI) exist as potential iron sources PMID: 25649872
Transferrin and thyroid hormone converge to regulate oligodendrocyte maturation and myelinogenesis. PMID: 25595122
This evidence supports a key role of Tf on the generation of oligodendrocytes (OLs) from Neural stem and progenitor cells (NSC/NPCs)and highlights its potential in demyelinating disorder treatment. PMID: 22479482
Transferrin is involved in the uptake of the radiopharmaceutical gallium-67 (67Ga) by regenerating liver tissue following partial hepatectomy but is not involved in the entry of 67Ga into hepatocytes. PMID: 11767098
data show that brain cells have the capacity to maintain minimum iron levels during iron deficiency which may be associated with increased iron-Tf uptake, stabilization of TfR mRNA, or increased Tf mRNA translation efficiency in specific cell types PMID: 12608731
effects of apotransferrin occur early in development during a narrow, transient "temporal window" within which oligodendroglia are sensitive to its action. PMID: 12730961
first report describing presence of serotransferrin precursor protein homolog belonging to transferrin family and sharing epitopes with melanotransferrin in adrenal, its induction by ACTH, and sensitivity to ginkgolide B (adrenotransferrin). PMID: 14701678
compared to transferrin, soluble melanotransferrin plays little or no role in Fe supply to the brain and erythropoietic tissue PMID: 15469901
in addition to hemoglobin-bound iron, Tf-bound iron may contribute to intracerebral hemorrhage-induced brain injury and thrombin may contribute to the latter by facilitating cellular iron uptake PMID: 15637325
Our studies suggest that AEC I is not just a simple barrier for gas exchange, but a functional cell that protects alveolar epithelium from injury. PMID: 16497717
Plays role in maturation of Schwann cells(SC) in physiological conditions as well as in role in facilitating clearance of myelin debris and subsequent nerve regeneration and/or in SC phenotypic change, which led to survival after peripheral nerve injury. PMID: 17628542
Apotransferrin added to oligodendroglial cell cultures can correct the effects of iron deficiency. PMID: 18459135
serotransferrin levels were increased in diestrous as compared with proestrous, estrous, metestrous PMID: 18511206
we have discovered a novel mitochondrial iron transport system that goes awry in Parkinson's disease, and which may provide a new target for therapeutic intervention. PMID: 19250966
synthesis and secretion of transferrin in rat parotid acinar cells PMID: 19464997

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.