Recombinant Human Inhibin Beta E Chain (INHBE) Protein (His)

Name: Recombinant Human Inhibin Beta E Chain (INHBE) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06564P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Inhibin Beta E Chain (INHBE) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P58166
Target Symbol	INHBE
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	TPTCEPATPLCCRRDHYVDFQELGWRDWILQPEGYQLNYCSGQCPPHLAGSPGIAASFHSAVFSLLKANNPWPASTSCCVPTARRPLSLLYLDHNGNVVKTDVPDMVVEACGCS
Expression Range	237-350aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.4 kDa
Research Area	Signal Transduction
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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	Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular Location	Secreted.
Protein Families	TGF-beta family
Database References	HGNC: 24029 OMIM: 612031 KEGG: hsa:83729 STRING: 9606.ENSP00000266646 UniGene: Hs.632713

Gene Functions References

INHBE functions as a possible hepatokine to alter the whole-body metabolic status under obese insulin-resistant condition PMID: 29596463
Activin A, B, and AB have similar effects on steroidogenesis in human granulosa cells; in contrast, activin AC is not biologically active and does not act as a competitive antagonist. PMID: 25062451
The inhibin-betaC subunit is down-regulated, while inhibin-betaE is up-regulated by interferon-beta1a in Ishikawa carcinoma cell line. PMID: 23580013
differential expression pattern of the betaC- and betaE-subunits in normal human endometrial tissue suggests that they function in endometrial maturation and blastocyst implantation. PMID: 21092084
Expression of the inhibin betaC and betaE subunits was demonstrated at the protein level and at the transcriptional level in normal human endometrial tissue and in the Ishikawa human endometrial carcinoma cell line. PMID: 20012305
An immunolabelling of the inhibin-betaE subunit in normal and malignant cervical tissue, as well as cervical cancer cells, is demonstrated. PMID: 20033758
cDNA cloning from a liver cDNA library, deduction of amino acid sequence, binding to follistatin, and analysis of the transcript in human liver PMID: 12242034
activin E has a role in regulating the proliferation of pancreatic exocrine cells PMID: 16426570

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.